Cohesin

This article is about the protein complex. For the protein domain in cellulose degrading bacteria, see Cohesin domain.

Diagram of cohesin showing its four constituent protein subunits

Cohesin is a protein complex that mediates sister chromatid cohesion, homologous recombination, and DNA looping. Cohesin is formed of SMC3, SMC1, SCC1 and SCC3 (SA1 or SA2 in humans). Cohesin holds sister chromatids together after DNA replication until anaphase when removal of cohesin leads to separation of sister chromatids. The complex forms a ring-like structure and it is believed that sister chromatids are held together by entrapment inside the cohesin ring. Cohesin is a member of the SMC family of protein complexes which includes Condensin, MukBEF and SMC-ScpAB.

Cohesin was separately discovered in budding yeast ( Saccharomyces cerevisiae ) both by Douglas Koshland ^[1] and Kim Nasmyth in 1997. ^[2]

Structure and subuntis

Models of SMC and cohesin structure

Main article: SMC_protein § Molecular_structure

Cohesin is a multi-subunit protein complex, made up of SMC1, SMC3, RAD21 and SCC3 (SA1 or SA2). ^[3] SMC1 and SMC3 are members of the Structural Maintenance of Chromosomes (SMC) family. SMC proteins have two main structural characteristics: an ATP-binding cassette-like 'head' domain with ATPase activity (formed by the interaction of the N- and C- terminals) and a hinge domain that allows dimerization of SMCs. The head and the hinge domains are connected to each other via long anti-parallel coiled coils. The dimer is present in a V-shaped form, connected by the hinges.

The N-terminal domain of RAD21 contains two α-helices which forms a three helix bundle with the coiled coil of SMC3. ^[4] The central region of RAD21 is thought to be largely unstructured but contains several binding sites for regulators of cohesin. This includes a binding site for SA1 or SA2, ^[5] recognition motifs for separase cleavage ^[6] and a region that is competitively bound by PDS5A, PDS5B or NIPBL. ^{[7] [8] [9]} The C-terminal domain of RAD21 forms a winged helix that binds two β-sheets in the Smc1 head domain. ^[10]

Once RAD21 binds the SMC proteins, SCC3 can also associate with RAD21. When RAD21 binds on both SMC1 and SMC3, the cohesin complex forms a closed ring structure. The interfaces between the SMC subunits and RAD21 can open to allow DNA to pass in and out of the cohesin ring. ^[11]

A structure of the entire cohesin complex has been solved using cryo-electron microscopy. ^[12] Key findings from the structural studies include:

1. Ring Architecture. Cohesin forms a tripartite ring where the SMC proteins (SMC1 and SMC3) dimerize via their hinge domains and are bridged by RAD21.
2. ATPase Domain. The head domains of SMC proteins contain ATPase sites that drive cohesin's dynamic interactions with DNA, mostly loop extrusion.
3. Conformational Flexibility. Cohesin is a highly dynamic protein, which exist in the open and closed conformations, interchanging by bending in the so-called elbows (see Loop extrusion for more).
4. Regulatory Interactions. Accessory proteins like WAPL and PDS5 have been visualized interacting with the cohesin complex, elucidating their roles in unloading and stabilizing cohesin on chromatin.

Function

Cohesin functions can broadly separated into two categories: roles in trans (between different chromosomes due to cohesion between them) and in cis (within the same chromosome due to loop extrusion). ^[13] Although these two functions are tightly interlinked, it has been possible to separate them by creating a cohesin hinge mutant that can extrude loops but cannot maintain cohesion. ^[13]

Role in chromatin compaction and global organization

1. DNA compaction. Cohesin helps to compact DNA by creating the loops of DNA in an ATP-dependent manner via the process called loop extrusion.
2. Segregation of chromosomes. Cohesin's activity promotes segregation of chromosomes into chromosomal territories. ^[14]

Role in cell division

Cohesin plays an important role in cell division in both mitosis and meiosis.

• During mitosis:
  1. Maintains sister chromatid cohesion. Cohesin keeps the sister chromatids connected during metaphase ensuring that each sister chromatid segregates to opposite poles during cell division. Without cohesin, the cell would be unable to control sister chromatid segregation since there would be no way of ensuring whether the spindle fiber—attached on each sister chromatid—is from a different pole. ^{[15] [16]} Other proteins modulate cohesin function by regulating this process, such as PDS5A, PDS5B, NIPBL and ESCO1 in mammalian cells. ^[16]
  2. Helps to assemble bipolar spindle apparatus. Cohesin ensures the attachment of spindle microtubules and sister kinetochores onto the chromosomes. This is tightly related to the correct sister chromatid segregation towards the two spindle poles. Dysregulation of this process leads to premature chromosomes separation and multipolar spindle-formation. ^{[17] [18]} The proteins Shugoshin 1 (or SGO1), Rae1 and NuMA are associated with cohesin in this assembly process. ^{[19] [20]}
• During meiosis, cohesin recruits additional meiotic-specific component Rec8, that is an essential player in these three processes: ^[21]
  1. Sister chromatids cohesion.
  2. Homologous chromosomes pairing.
  3. Recombination during meiosis.

Cohesin has also been found to be crucial for DNA damage checkpoint and repair. It participates in repairing double-strand breaks in DNA via homologous recombination, where the sister chromatid is used as a template for sequence reconstruction. ^[22]

Role in regulation

Cohesin might play an important role in regulation of gene expression through the following mechanisms:

1. Cohesin mediating enhancer-promoter interactions by bridging them in cis. ^[23]
2. Cohesin connecting CTCF sites in cis by interacting with CTCFs in a highly specific and oriented manner. ^[24]
3. Cohesin creating regulatory TADs ^[25] which are the environments for promoter-enhancer interactions. ^[26]

Other functions

• Cohesin has been found to be essential for embryo development. Cohesin knockout is lethal for development of mouse and zebrafish. ^{[27] [28]}
• Cohesin deletion in mature macrophages leads to impairment of inflammatory response of the innate immune system and restricts transcriptional response of primary macrophages to microbial signals. ^[29]

Localization on DNA

Cohesin binding along the chromosomal DNA is considered to be dynamic and its location changes based on gene transcription, specific DNA sequence and presence of chromosome-associated proteins. There are several observations on cohesin patterns of localization on DNA.

• Accumulation at CTCF sites: This happens due to direct interaction of cohesin subunits SA2 and SCC1 with CTCF. ^[30] Briefly, in the process of loop extrusion, cohesin moves actively along the two DNA double helices, translocating one of them with respect to the other. Thus, the loop can become smaller or larger. The loop extrusion process stops when cohesin encounters the architectural chromatin protein CTCF. The CTCF site needs to be in a proper orientation to stop cohesin. ^{[31] [32] [33]}
• Accumulation at promoters: Two hypotheses were proposed to explain accumulation of cohesin at the gene promoters: ^{[34] [35]}

1. Cohesin location is influenced by the orientation of neighboring genes and it is most frequently located in areas of convergent transcription. Gene orientation depends on the direction of transcription and can be of three types: head-to-head, head-to-tail and tail-to-tail. The tail-to-tail configuration results in the convergence of transcription machinery. One hypothesis states that the RNA polymerase “pushes” cohesin along the DNA, causing them to move towards the direction of the RNA polymerases. Changing the transcription pattern of genes changes the location of cohesin indicating that localization of cohesin may depend on transcription. ^[36]
2. In another model, chromatin loop extrusion is pushed by transcription generated supercoiling ensuring also that cohesin relocalizes quickly and loops grow with reasonable speed and in a good direction. In addition, the supercoiling-driven loop extrusion mechanism is consistent with earlier explanations proposing why topologically associating domains (TADs) flanked by convergent CTCF binding sites form more stable chromatin loops than TADs flanked by divergent CTCF binding sites. In this model, the supercoiling also stimulates enhancer promoter contacts and it is proposed that transcription of eRNA sends the first wave of supercoiling that can activate mRNA transcription in a given TAD. ^[37]

• Accumulation AT-rich sequences: Cohesins can be frequently found in chromosome arms that have AT-rich DNA sequences indicating that DNA sequence may be an independent factor of cohesin binding. ^[36]
• Accumulation at centromeres: Cohesin rings, especially in budding yeast, are also located in the region surrounding the centromere. ^[36] Two hypotheses may explain this: the presence of repetitive heterochromatic DNA in centromeres and the presence of chromosome-associated proteins. For example, Schizosaccharomyces pombe have multiple copies of specific heterochromatic DNA whose involvement in cohesion binding has been proven. Budding yeast lacks repetitive sequences and, therefore, requires a different mechanism for cohesion binding. Evidence suggests that binding of cohesin to the budding yeast centromere region depends on chromosome-associated proteins of the kinetochore that mediate cohesion association to pericentric regions (the kinetochore is an enhancer of pericentric cohesin binding). ^[38]

Cohesin in sister chromatid cohesion

Main article: Establishment of sister chromatid cohesion

Mechanism of sister chromatid cohesion

It is not clear how the cohesin ring links sister chromatids together. There are two possible scenarios:

1. Cohesin subunits bind to each sister chromatid and form a bridge between the two.
2. Since cohesin has a ring structure, it is able to encircle both sister chromatids.

Current evidence suggests that the second scenario is the most likely. Proteins that are essential for sister chromatid cohesion, such as Smc3 and Scc1, do not regulate the formation of covalent bonds between cohesin and DNA, indicating that DNA interaction is not sufficient for cohesion. ^[11] In addition, disturbing the ring structure of cohesin through cleavage of Smc3 or Scc1 triggers premature sister chromatid segregation in vivo. ^[39] This shows that the ring structure is important for cohesin's function.

Early studies suggested various ways in which cohesin may entrap DNA, ^[40] including as a monomer that holds both homologues together, and a "hand-cuff" model where two intertwining cohesin complexes each hold one sister chromatid. While some studies support the idea of a hand-cuff model, ^[40] the model is inconsistent with a number of experimental observations, ^[41] and is generally considered to entrap chromatin as a monomer.

Even though the ring hypothesis appears to be valid, there are still questions about the number of rings required to hold sister chromatids together. One possibility is that one ring surrounds the two chromatids. Another possibility involves the creation of a dimer where each ring surrounds one sister chromatid. The two rings are connected to each other through formation of a bridge that holds the two sister chromatids together.

The topology and structure of these subunits has been best characterized in budding yeast, ^{[42] [43]} but the sequence conservation of these proteins and biochemical and electron microscopic observations imply that cohesin complexes in other species are very similar in their structure .

The cohesin complex is established during the initial stages of S-phase. The complexes associate with chromosomes before DNA replication occurs. Once cells start replicating their DNA, cohesin rings close and link the sister chromatids together. ^[11] Cohesin complexes must be present during S-phase in order for cohesion to take place. It is unclear, however, how cohesin is loaded on the chromosomes during G1. There are two proposed hypotheses so far:

1. The ATPase domain of the SMC proteins interacts with DNA and this interaction initially mediates the loading of cohesin complexes on chromosomes.
2. Several proteins aid in the loading process. For example, Scc2 and Scc4 are both required for cohesin to load in budding yeast.

Dissociation of sister chromatid cohesion

The anaphase promoting complex associated to Cdc20 (APC/C-cdc20) marks Securin (anaphase inhibitor) for degradation by the proteasome. Securin is cleaved at anaphase, following APC/C-cdc20 mediated degradation, and it renders separase (a protease, inhibited by the association with securin) to cleave the kleisin subunit. An alpha-kleisin is associated with the cohesin complex, linking both SMC 3 and SMC 1 together, with the exact kleisin varying between mitosis and meiosis (Scc1 and Rec8 respectively), and its cleavage ultimately leads to the removal of cohesin from chromosomes. ^[44]

Dissociation of sister chromatids cohesion defines anaphase onset, which establishes two sets of identical chromosomes at each pole of the cell (telophase). Then the two daughter cells separate, and a new round of the cell cycle freshly starts in each one, at the stage of G0. When cells are ready to divide, because cell size is big enough or because they receive the appropriate stimulus, ^[45] they activate the mechanism to enter into the G1 stage of cell cycle, and they duplicate most organelles during S (synthesis) phase, including their centrosome. Therefore, when the cell division process will end, each daughter cell will receive a complete set of organelles. At the same time, during S phase all cells must duplicate their DNA very precisely, a process termed DNA replication. Once DNA replication has finished, in eukaryotes the DNA molecule is compacted and condensed, to form the mitotic chromosomes, each one constituted by two sister chromatids, which stay held together by the establishment of cohesion between them; each chromatid is a complete DNA molecule, attached via microtubules to one of the two centrosomes of the dividing cell, located at opposed poles of the cell. To avoid premature sister chromatid separation, the APC/C is maintained in an inactive state bound to different molecules, which are part of a complex mechanism termed the spindle assembly checkpoint.

Cohesin in meiosis

Cohesin proteins SMC1β, SMC3, REC8 and STAG3 appear to participate in cohesion of sister chromatids throughout the meiotic process in human oocytes. ^[46] SMC1β, REC8 and STAG3 proteins are meiosis specific cohesins.

The STAG3 protein appears to be essential for female meiosis. A homozygous frameshift mutation in the Stag3 gene was identified in a large consanguineous family with premature ovarian failure. ^[47] Also, female mice deficient in STAG3 are sterile, and their fetal oocytes arrest at early prophase 1.

During meiosis, establishment of cohesion of sister chromatids via cohesin rings is necessary for ensuring homologous recombination-mediated DNA repair and subsequent proper chromosome segregation. ^[48] The cohesin proteins are loaded on to chromatids during female fetal life and are not replenished over time, and thus with advancing maternal age aneuploidy in oocytes tends to increase resulting in decreased fecundity and increased infertility and miscarriage. ^[48] Also, variants of cohesin proteins are associated with primary ovarian insufficiency, trisomy in offspring and non-obstructive azoospermia. ^[48]

Oocyte loss is a natural process that accelerates as women enter their mid-thirties, and thus has a significant effect on female reproduction. Aged oocytes have a lower DNA repair capacity linked to cohesin deterioration. ^[49] Reduced cohesin levels make aged oocytes more vulnerable to persistent DNA damage leading to oocyte loss. ^[49]

Cohesin in loop extrusion

Main article: Loop extrusion

Loop extrusion, an ATP-dependent process driven by SMC-family proteins like cohesin and condensin, involves the translocation of DNA to form loops. This process continues until the extruding complex is released or encounters a barrier. In vertebrates, one well-studied factor that limits loop extrusion by cohesin is the CCCTC-binding factor (CTCF). CTCF directly interacts with cohesin, stabilizing it on chromatin and anchoring loop boundaries. ^{[50] [51]} The loop extrusion process leads to the formation of topologically associating domains (TADs) and loops in interphase. ^[24]

Evolution

The SMC proteins are found across the tree of life as early as in prokaryotes and have been conserved through evolution. In particular, the coils of SMC1 and SMC3 are conserved with an amino acid divergence of less than 0.5%. ^[52]

In bacteria, SMC-like protein MukBEF is involved in chromosome compaction ^[53] and segregation. ^[54] Most cohesin subunits are present in different eukaryotic taxa. ^[55] However, although uniformly present, cohesin might have different functions in different taxa. For example, in Drosophila melanogaster the extruding role of cohesin is debatable. ^[56]

Cohesin subunits in different eukaryotes may have different names:

Name	Saccharomyces cerevisiae	Schizosaccharomyces pombe	Drosophila	Vertebrates
Smc1	Smc1	Psm1	DmSmc1	Smc1
Smc3	Smc3	Psm3	Cap	Smc3
α-Kleisin subunit	Mcd1/Pds3/Scc1	Rad21	DmRad21	Rad21
Stromalin subunits	Scc3	Psc3	DmSA	SA1 and SA2/STAG1 and STAG2
Scc2	Scc2		Nipped-B	NIPBL
Scc4	Scc4		Mau2	MAU2
PDS5	PDS5		Pds5	PDS5A
Wapl	Rad61/Wpl1		Wapl	WAPL
Cohesin acetyl transferase (CoAT)	ECO1/CTF7		Deco/San	ESCO1 and ESCO2
Cohesin deacetylase (CoDAC)	Hos1		?	HDAC8

Research techniques to study cohesin

• Chromatin Immunoprecipitation (ChIP): Used to study cohesin-DNA interactions. Includes variations, such as ChIP-chip ^[57] or, more recent whole-genome ChIP-Seq. ^[58]
• Chromosomes conformation capture : Used to analyze formation of loops and TADs that are frequently mediated by cohesin. This includes 3C, ^[59] and more recent whole-genome versions Hi-C ^[60] and Micro-C. ^{[61] [62]} Notably, rapid degradation ^[63] of cohesin lead to drastic changes in Hi-C interaction patterns, such as change of chromatin scaling and disappearance of most TADs and dots.
• CRISPR/Cas9: Enables the study of cohesin mutations and functional analysis. ^[64]
• Live-cell imaging: Visualizes cohesin dynamic on chromatin. ^{[65] [66] [67]}

Clinical significance

Cohesinopathies

The term "cohesinopathy" has been used to describe conditions affecting the cohesin complex. ^{[68] [69] [70]}

These conditions include:

• Cornelia de Lange Syndrome (CdLS)
  • Cause: Mutations in NIPBL, SMC1A, SMC3, HDAC8, and RAD21. ^[71]
  • Symptoms: Growth retardation, intellectual disability, and limb deformities among others.
• Roberts syndrome (RBS)
  • Cause: Mutations in ESCO2, impairing cohesin acetylation. ^[72]
  • Symptoms: Prenatal growth failure, craniofacial abnormalities, and limb malformations.
• Warsaw breakage syndrome (WABS)
  • Cause: Mutations in DDX11, a helicase interacting with cohesin. ^[73]
  • Symptoms: Chromosomal instability, intellectual disability, and growth defects.

Cohesin in cancer

Cohesin mutations are frequently observed in cancers such as acute myeloid leukemia (AML), myelodysplastic syndromes (MDS), colorectal cancer, glioblastoma and bladder cancer. ^[74] Among the cohesin genes, STAG2 is the most commonly mutated, accounting for approximately half of all cohesin-related mutations observed in cancer. ^[75]

• STAG2 mutations are linked to chromosomal instability and poor prognosis in AML and MDS. ^[76]
• Disruption of DNA repair due to cohesin loss contributes to increased mutational burden in tumors. ^[76]

Other

The cohesin subunit STAG2 appears to play a significant role in hematopoietic function, as its loss enhances stem cell self-renewal while impairing differentiation. ^[77]

See also

• Condensin
• SMC protein
• Establishment of sister chromatid cohesion
• Loop extrusion

References

1. Guacci, V; Koshland, D; Strunnikov, A (3 October 1997). "A direct link between sister chromatid cohesion and chromosome condensation revealed through the analysis of MCD1 in S. cerevisiae". Cell. 91 (1): 47–57. doi:10.1016/s0092-8674(01)80008-8. PMC   2670185 . PMID   9335334.
2. Michaelis, C; Ciosk, R; Nasmyth, K (3 October 1997). "Cohesins: chromosomal proteins that prevent premature separation of sister chromatids". Cell. 91 (1): 35–45. doi: 10.1016/s0092-8674(01)80007-6 . PMID   9335333. S2CID   18572651.
3. Losada A, Hirano M, Hirano T (1998). "Identification of Xenopus SMC protein complexes required for sister chromatid cohesion". Genes Dev. 12 (13): 1986–1997. doi:10.1101/gad.12.13.1986. PMC   316973 . PMID   9649503.
4. Gligoris, TG; Scheinost, JC; Bürmann, F; Petela, N; Chan, KL; Uluocak, P; Beckouët, F; Gruber, S; Nasmyth, K; Löwe, J (21 November 2014). "Closing the cohesin ring: structure and function of its Smc3-kleisin interface". Science. 346 (6212): 963–7. Bibcode:2014Sci...346..963G. doi:10.1126/science.1256917. PMC   4300515 . PMID   25414305.
5. Hara, K; Zheng, G; Qu, Q; Liu, H; Ouyang, Z; Chen, Z; Tomchick, DR; Yu, H (October 2014). "Structure of cohesin subcomplex pinpoints direct shugoshin-Wapl antagonism in centromeric cohesion". Nature Structural & Molecular Biology. 21 (10): 864–70. doi:10.1038/nsmb.2880. PMC   4190070 . PMID   25173175.
6. Uhlmann, F; Lottspeich, F; Nasmyth, K (1 July 1999). "Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1". Nature. 400 (6739): 37–42. Bibcode:1999Natur.400...37U. doi:10.1038/21831. PMID   10403247. S2CID   4354549.
7. Petela, NJ; Gligoris, TG; Metson, J; Lee, BG; Voulgaris, M; Hu, B; Kikuchi, S; Chapard, C; Chen, W; Rajendra, E; Srinivisan, M; Yu, H; Löwe, J; Nasmyth, KA (21 June 2018). "Scc2 Is a Potent Activator of Cohesin's ATPase that Promotes Loading by Binding Scc1 without Pds5". Molecular Cell. 70 (6): 1134–1148.e7. doi: 10.1016/j.molcel.2018.05.022 . PMC   6028919 . PMID   29932904.
8. Kikuchi, S; Borek, DM; Otwinowski, Z; Tomchick, DR; Yu, H (1 November 2016). "Crystal structure of the cohesin loader Scc2 and insight into cohesinopathy". Proceedings of the National Academy of Sciences of the United States of America. 113 (44): 12444–12449. Bibcode:2016PNAS..11312444K. doi: 10.1073/pnas.1611333113 . PMC   5098657 . PMID   27791135.
9. Muir, KW; Kschonsak, M; Li, Y; Metz, J; Haering, CH; Panne, D (8 March 2016). "Structure of the Pds5-Scc1 Complex and Implications for Cohesin Function". Cell Reports. 14 (9): 2116–2126. doi: 10.1016/j.celrep.2016.01.078 . PMID   26923589.
10. Haering, CH; Schoffnegger, D; Nishino, T; Helmhart, W; Nasmyth, K; Löwe, J (24 September 2004). "Structure and stability of cohesin's Smc1-kleisin interaction" (PDF). Molecular Cell. 15 (6): 951–64. doi:10.1016/j.molcel.2004.08.030. PMID   15383284.
11. Gruber S, Haering CH, Nasmyth K (March 2003). "Chromosomal cohesin forms a ring". Cell. 112 (6): 765–77. doi: 10.1016/S0092-8674(03)00162-4 . PMID   12654244.
12. Shi, Zhubing; Gao, Haishan; Bai, Xiao-chen; Yu, Hongtao (2020-06-26). "Cryo-EM structure of the human cohesin-NIPBL-DNA complex". Science. 368 (6498): 1454–1459. Bibcode:2020Sci...368.1454S. doi:10.1126/science.abb0981. PMID   32409525.
13. Nagasaka, Kota; Davidson, Iain F.; Stocsits, Roman R.; Tang, Wen; Wutz, Gordana; Batty, Paul; Panarotto, Melanie; Litos, Gabriele; Schleiffer, Alexander; Gerlich, Daniel W.; Peters, Jan-Michael (2023). "Cohesin mediates DNA loop extrusion and sister chromatid cohesion by distinct mechanisms". Molecular Cell. 83 (17): 3049–3063.e6. bioRxiv   10.1101/2022.09.23.509019 . doi: 10.1016/j.molcel.2023.07.024 . PMID   37591243.
14. Goloborodko, Anton; Imakaev, Maxim V.; Marko, John F.; Mirny, Leonid (18 May 2016). "Compaction and segregation of sister chromatids via active loop extrusion". eLife. 5: e14864. doi: 10.7554/eLife.14864 . PMC   4914367 . PMID   27192037.
15. Nasmyth, Kim; Haering, Christian H. (2009). "Cohesin: its roles and mechanisms". Annual Review of Genetics. 43: 525–558. doi:10.1146/annurev-genet-102108-134233. PMID   19886810.
16. Brooker, Amanda S.; Berkowitz, Karen M. (2014). "The roles of cohesins in mitosis, meiosis, and human health and disease". Cell Cycle Control. Methods in Molecular Biology (Clifton, N.J.). Vol. 1170. pp. 229–266. doi:10.1007/978-1-4939-0888-2_11. ISBN   978-1-4939-0887-5. PMC   4495907 . PMID   24906316.
17. Wong, Richard W.; Blobel, Günter (2008-10-07). "Cohesin subunit SMC1 associates with mitotic microtubules at the spindle pole". Proceedings of the National Academy of Sciences of the United States of America. 105 (40): 15441–15445. Bibcode:2008PNAS..10515441W. doi: 10.1073/pnas.0807660105 . PMC   2557025 . PMID   18832153.
18. McNally, Karen P.; Beath, Elizabeth A.; Danlasky, Brennan M.; Barroso, Consuelo; Gong, Ting; Li, Wenzhe; Martinez-Perez, Enrique; McNally, Francis J. (October 2022). "Cohesin is required for meiotic spindle assembly independent of its role in cohesion in C. elegans". PLOS Genetics. 18 (10): e1010136. doi: 10.1371/journal.pgen.1010136 . PMC   9632809 . PMID   36279281.
19. McGuinness, Barry E.; Hirota, Toru; Kudo, Nobuaki R.; Peters, Jan-Michael; Nasmyth, Kim (March 2005). "Shugoshin prevents dissociation of cohesin from centromeres during mitosis in vertebrate cells". PLOS Biology. 3 (3): e86. doi: 10.1371/journal.pbio.0030086 . PMC   1054882 . PMID   15737064.
20. Kong, Xiangduo; Ball, Alexander R.; Sonoda, Eiichiro; Feng, Jie; Takeda, Shunichi; Fukagawa, Tatsuo; Yen, Tim J.; Yokomori, Kyoko (March 2009). "Cohesin associates with spindle poles in a mitosis-specific manner and functions in spindle assembly in vertebrate cells". Molecular Biology of the Cell. 20 (5): 1289–1301. doi:10.1091/mbc.e08-04-0419. PMC   2649254 . PMID   19116315.
21. Sakuno, Takeshi; Hiraoka, Yasushi (22 January 2022). "Rec8 cohesin: A structural platform for shaping the meiotic chromosomes". Genes. 13 (2): 200. doi: 10.3390/genes13020200 . PMC   8871791 . PMID   35205245.
22. Litwin, Ireneusz; Pilarczyk, Ewa; Wysocki, Robert (2018-11-28). "The Emerging Role of Cohesin in the DNA Damage Response". Genes. 9 (12): 581. doi: 10.3390/genes9120581 . PMC   6316000 . PMID   30487431.
23. Kane, Lauren; Williamson, Iain; Flyamer, Ilya M.; Kumar, Yatendra; Hill, Robert E.; Lettice, Laura A.; Bickmore, Wendy A. (September 2022). "Cohesin is required for long-range enhancer action at the Shh locus". Nature Structural & Molecular Biology. 29 (9): 891–897. doi:10.1038/s41594-022-00821-8. PMC   7613721 . PMID   36097291.
24. Rao, Suhas S.P.; Huntley, Miriam H.; Durand, Neva C.; Stamenova, Elena K.; Bochkov, Ivan D.; Robinson, James T.; Sanborn, Adrian L.; Machol, Ido; Omer, Arina D.; Lander, Eric S.; Aiden, Erez Lieberman (18 December 2014). "A 3D map of the human genome at kilobase resolution reveals principles of chromatin looping". Cell. 159 (7): 1665–1680. doi:10.1016/j.cell.2014.11.021. PMC   5635824 . PMID   25497547.
25. Rao, Suhas S.P.; Huang, Su-Chen; Glenn St Hilaire, Brian; Engreitz, Jesse M.; Perez, Elizabeth M.; Kieffer-Kwon, Kyong-Rim; Sanborn, Adrian L.; Johnstone, Sarah E.; Bascom, Gavin D.; Bochkov, Ivan D.; Huang, Xingfan; Shamim, Muhammad S.; Shin, Jaeweon; Turner, Douglass; Ye, Ziyi; Omer, Arina D.; Robinson, James T.; Schlick, Tamar; Bernstein, Bradley E.; Casellas, Rafael; Lander, Eric S.; Aiden, Erez Lieberman (5 October 2017). "Cohesin loss eliminates all loop domains". Cell. 171 (2): 305–320.e24. doi:10.1016/j.cell.2017.09.026. PMC   5846482 . PMID   28985562.
26. Lupiáñez, Darío G.; Kraft, Katerina; Heinrich, Verena; Krawitz, Peter; Brancati, Francesco; Klopocki, Eva; Horn, Denise; Kayserili, Hülya; Opitz, John M.; Laxova, Renata; Santos-Simarro, Fernando; Gilbert-Dussardier, Brigitte; Wittler, Lars; Borschiwer, Marina; Haas, Stefan A.; Osterwalder, Marco; Franke, Martin; Timmermann, Bernd; Hecht, Jochen; Spielmann, Malte; Visel, Axel; Mundlos, Stefan (21 May 2015). "Disruptions of topological chromatin domains cause pathogenic rewiring of gene-enhancer interactions". Cell. 161 (5): 1012–1025. doi:10.1016/j.cell.2015.04.004. PMC   4791538 . PMID   25959774.
27. Horsfield, Julia A.; Print, Cristin G.; Mönnich, Maren (2012). "Diverse Developmental Disorders from the One Ring: Distinct Molecular Pathways Underlie the Cohesinopathies". Frontiers in Genetics. 3: 171. doi: 10.3389/fgene.2012.00171 . PMC   3439829 . PMID   22988450.
28. Chin, Chue Vin; Antony, Jisha; Ketharnathan, Sarada; Labudina, Anastasia; Gimenez, Gregory; Parsons, Kate M.; He, Jinshu; George, Amee J.; Pallotta, Maria Michela; Musio, Antonio; Braithwaite, Antony; Guilford, Parry; Hannan, Ross D.; Horsfield, Julia A. (7 December 2020). "Cohesin mutations are synthetic lethal with stimulation of WNT signaling". eLife. 9: e61405. doi: 10.7554/eLife.61405 . PMC   7746233 . PMID   33284104.
29. Cuartero, Sergi; Weiss, Felix D.; Dharmalingam, Gopuraja; Guo, Ya; Ing-Simmons, Elizabeth; Masella, Silvia; Robles-Rebollo, Irene; Xiao, Xiaolin; Wang, Yi-Fang; Barozzi, Iros; Djeghloul, Dounia; Amano, Mariane T.; Niskanen, Henri; Petretto, Enrico; Dowell, Robin D.; Tachibana, Kikuë; Kaikkonen, Minna U.; Nasmyth, Kim A.; Lenhard, Boris; Natoli, Gioacchino; Fisher, Amanda G.; Merkenschlager, Matthias (September 2018). "Control of inducible gene expression links cohesin to hematopoietic progenitor self-renewal and differentiation". Nature Immunology. 19 (9): 932–941. doi:10.1038/s41590-018-0184-1. PMC   6195188 . PMID   30127433.
30. Li, Yan; Haarhuis, Judith H. I.; Sedeño Cacciatore, Ángela; Oldenkamp, Roel; van Ruiten, Marjon S.; Willems, Laureen; Teunissen, Hans; Muir, Kyle W.; de Wit, Elzo; Rowland, Benjamin D.; Panne, Daniel (February 2020). "The structural basis for cohesin–CTCF-anchored loops". Nature. 578 (7795): 472–476. Bibcode:2020Natur.578..472L. doi:10.1038/s41586-019-1910-z. PMC   7035113 . PMID   31905366.
31. Fudenberg, Geoffrey; Imakaev, Maxim; Lu, Carolyn; Goloborodko, Anton; Abdennur, Nezar; Mirny, Leonid A. (May 2016). "Formation of Chromosomal Domains by Loop Extrusion". Cell Reports. 15 (9): 2038–2049. doi:10.1016/j.celrep.2016.04.085. PMC   4889513 . PMID   27210764.
32. Valton, Anne-Laure; Venev, Sergey V.; Mair, Barbara; Khokhar, Eraj Shafiq; Tong, Amy H. Y.; Usaj, Matej; Chan, Katherine; Pai, Athma A.; Moffat, Jason; Dekker, Job (December 2022). "A cohesin traffic pattern genetically linked to gene regulation". Nature Structural & Molecular Biology. 29 (12): 1239–1251. doi:10.1038/s41594-022-00890-9. PMC   10228515 . PMID   36482254.
33. Busslinger, Georg A.; Stocsits, Roman R.; van der Lelij, Petra; Axelsson, Elin; Tedeschi, Antonio; Galjart, Niels; Peters, Jan-Michael (April 2017). "Cohesin is positioned in mammalian genomes by transcription, CTCF and Wapl". Nature. 544 (7651): 503–507. Bibcode:2017Natur.544..503B. doi:10.1038/nature22063. PMC   6080695 . PMID   28424523.
34. Banigan, Edward J.; Tang, Wen; van den Berg, Aafke A.; Stocsits, Roman R.; Wutz, Gordana; Brandão, Hugo B.; Busslinger, Georg A.; Peters, Jan-Michael; Mirny, Leonid A. (2023-03-14). "Transcription shapes 3D chromatin organization by interacting with loop extrusion". Proceedings of the National Academy of Sciences. 120 (11): e2210480120. Bibcode:2023PNAS..12010480B. doi:10.1073/pnas.2210480120. PMC   10089175 . PMID   36897969.
35. Fursova, Nadezda A.; Larson, Daniel R. (2024-12-01). "Transcriptional machinery as an architect of genome structure". Current Opinion in Structural Biology. 89: 102920. doi:10.1016/j.sbi.2024.102920. PMID   39306948.
36. Ross KE, Cohen-Fix O (July 2004). "Molecular biology: cohesins slip sliding away". Nature. 430 (6999): 520–1. Bibcode:2004Natur.430..520R. doi: 10.1038/430520b . PMID   15282594. S2CID   52818523.
37. Racko D, Benedetti F, Dorier J, Stasiak A (13 November 2017). "Transcription-induced supercoiling as the driving force of chromatin loop extrusion during formation of TADs in interphase chromosomes". Nucleic Acids Res. 46 (4): 1648–1660. doi:10.1093/nar/gkx1123. PMC   5829651 . PMID   29140466.
38. Weber SA, Gerton JL, Polancic JE, DeRisi JL, Koshland D, Megee PC (September 2004). "The kinetochore is an enhancer of pericentric cohesin binding". PLOS Biology. 2 (9): E260. doi: 10.1371/journal.pbio.0020260 . PMC   490027 . PMID   15309047.
39. Peters JM, Tedeschi A, Schmitz J (November 2008). "The cohesin complex and its roles in chromosome biology". Genes & Development. 22 (22): 3089–114. doi: 10.1101/gad.1724308 . PMID   19056890.
40. Zhang N, Kuznetsov SG, Sharan SK, Li K, Rao PH, Pati D (December 2008). "A handcuff model for the cohesin complex". The Journal of Cell Biology. 183 (6): 1019–31. doi:10.1083/jcb.200801157. PMC   2600748 . PMID   19075111.
41. Nasmyth K (October 2011). "Cohesin: a catenase with separate entry and exit gates?". Nature Cell Biology. 13 (10): 1170–7. doi:10.1038/ncb2349. PMID   21968990. S2CID   25382204.
42. Haering, CH; Löwe, J; Hochwagen, A; Nasmyth, K (April 2002). "Molecular architecture of SMC proteins and the yeast cohesin complex". Molecular Cell. 9 (4): 773–88. doi: 10.1016/s1097-2765(02)00515-4 . PMID   11983169.
43. Haering, CH; Farcas, AM; Arumugam, P; Metson, J; Nasmyth, K (17 July 2008). "The cohesin ring concatenates sister DNA molecules" (PDF). Nature. 454 (7202): 297–301. Bibcode:2008Natur.454..297H. doi:10.1038/nature07098. PMID   18596691. S2CID   1190883.
44. Mehta GD, Rizvi SM, Ghosh SK (August 2012). "Cohesin: a guardian of genome integrity". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1823 (8): 1324–42. doi: 10.1016/j.bbamcr.2012.05.027 . PMID   22677545.
45. Conlon I, Raff M (January 1999). "Size control in animal development". Cell. 96 (2): 235–44. doi: 10.1016/S0092-8674(00)80563-2 . PMID   9988218.
46. Garcia-Cruz R, Brieño MA, Roig I, Grossmann M, Velilla E, Pujol A, Cabero L, Pessarrodona A, Barbero JL, Garcia Caldés M (September 2010). "Dynamics of cohesin proteins REC8, STAG3, SMC1 beta and SMC3 are consistent with a role in sister chromatid cohesion during meiosis in human oocytes". Human Reproduction. 25 (9): 2316–27. doi:10.1093/humrep/deq180. PMID   20634189.
47. Caburet S, Arboleda VA, Llano E, Overbeek PA, Barbero JL, Oka K, Harrison W, Vaiman D, Ben-Neriah Z, García-Tuñón I, Fellous M, Pendás AM, Veitia RA, Vilain E (March 2014). "Mutant cohesin in premature ovarian failure". The New England Journal of Medicine. 370 (10): 943–949. doi:10.1056/NEJMoa1309635. PMC   4068824 . PMID   24597867.
48. Beverley R, Snook ML, Brieño-Enríquez MA (2021). "Meiotic Cohesin and Variants Associated With Human Reproductive Aging and Disease". Front Cell Dev Biol. 9: 710033. doi: 10.3389/fcell.2021.710033 . PMC   8365356 . PMID   34409039.  This article incorporates textfrom this source, which is available under the CC BY 4.0 license.
49. Sharma N, Coticchio G, Borini A, Tachibana K, Nasmyth KA, Schuh M (November 2024). "Changes in DNA repair compartments and cohesin loss promote DNA damage accumulation in aged oocytes". Curr Biol. 34 (22): 5131–5148.e6. doi:10.1016/j.cub.2024.09.040. PMID   39437784.
50. Li, Yan; Haarhuis, Judith H. I.; Sedeño Cacciatore, Ángela; Oldenkamp, Roel; Van Ruiten, Marjon S.; Willems, Laureen; Teunissen, Hans; Muir, Kyle W.; De Wit, Elzo; Rowland, Benjamin D.; Panne, Daniel (February 2020). "The structural basis for cohesin-CTCF-anchored loops". Nature. 578 (7795): 472–476. Bibcode:2020Natur.578..472L. doi:10.1038/s41586-019-1910-z. PMC   7035113 . PMID   31905366.
51. Hansen, Anders S. (December 2020). "CTCF as a boundary factor for cohesin-mediated loop extrusion: evidence for a multi-step mechanism". Nucleus (Austin, Tex.). 11 (1): 132–148. doi:10.1080/19491034.2020.1782024. PMC   7566886 . PMID   32631111.
52. White GE, Erickson HP (2009). "The coiled coils of cohesin are conserved in animals, but not in yeast". PLOS ONE. 4 (3): e4674. Bibcode:2009PLoSO...4.4674W. doi: 10.1371/journal.pone.0004674 . PMC   2650401 . PMID   19262687.
53. Bürmann, Frank; Funke, Louise F.H.; Chin, Jason W.; Löwe, Jan (December 2021). "Cryo-EM structure of MukBEF reveals DNA loop entrapment at chromosomal unloading sites". Molecular Cell. 81 (23): 4891–4906.e8. doi:10.1016/j.molcel.2021.10.011. PMC   8669397 . PMID   34739874.
54. Niki, H.; Imamura, R.; Kitaoka, M.; Yamanaka, K.; Ogura, T.; Hiraga, S. (December 1992). "E.coli MukB protein involved in chromosome partition forms a homodimer with a rod-and-hinge structure having DNA binding and ATP/GTP binding activities". The EMBO Journal. 11 (13): 5101–5109. doi:10.1002/j.1460-2075.1992.tb05617.x. PMC   556988 . PMID   1464330.
55. Hoencamp, Claire; Dudchenko, Olga; Elbatsh, Ahmed M. O.; Brahmachari, Sumitabha; Raaijmakers, Jonne A.; van Schaik, Tom; Sedeño Cacciatore, Ángela; Contessoto, Vinícius G.; van Heesbeen, Roy G. H. P.; van den Broek, Bram; Mhaskar, Aditya N.; Teunissen, Hans; St Hilaire, Brian Glenn; Weisz, David; Omer, Arina D. (2021-05-28). "3D genomics across the tree of life reveals condensin II as a determinant of architecture type". Science. 372 (6545): 984–989. doi:10.1126/science.abe2218. PMC   8172041 . PMID   34045355.
56. Matthews, Nicholas E.; White, Rob (September 2019). "Chromatin Architecture in the Fly: Living without CTCF/Cohesin Loop Extrusion?: Alternating Chromatin States Provide a Basis for Domain Architecture in Drosophila". BioEssays. 41 (9): e1900048. doi: 10.1002/bies.201900048 . PMID   31264253.
57. Wendt, Kerstin S.; Yoshida, Keisuke; Itoh, Takehiko; Bando, Masashige; Koch, Birgit; Schirghuber, Erika; Tsutsumi, Shuichi; Nagae, Genta; Ishihara, Ko; Mishiro, Tsuyoshi; Yahata, Kazuhide; Imamoto, Fumio; Aburatani, Hiroyuki; Nakao, Mitsuyoshi; Imamoto, Naoko (February 2008). "Cohesin mediates transcriptional insulation by CCCTC-binding factor". Nature. 451 (7180): 796–801. Bibcode:2008Natur.451..796W. doi:10.1038/nature06634. PMID   18235444.
58. Tang, Zhonghui; Luo, Oscar Junhong; Li, Xingwang; Zheng, Meizhen; Zhu, Jacqueline Jufen; Szalaj, Przemyslaw; Trzaskoma, Pawel; Magalska, Adriana; Wlodarczyk, Jakub; Ruszczycki, Blazej; Michalski, Paul; Piecuch, Emaly; Wang, Ping; Wang, Danjuan; Tian, Simon Zhongyuan (December 2015). "CTCF-Mediated Human 3D Genome Architecture Reveals Chromatin Topology for Transcription". Cell. 163 (7): 1611–1627. doi:10.1016/j.cell.2015.11.024. PMC   4734140 . PMID   26686651.
59. Dekker, Job; Rippe, Karsten; Dekker, Martijn; Kleckner, Nancy (2002-02-15). "Capturing Chromosome Conformation". Science. 295 (5558): 1306–1311. Bibcode:2002Sci...295.1306D. doi:10.1126/science.1067799. PMID   11847345.
60. Lieberman-Aiden, Erez; van Berkum, Nynke L.; Williams, Louise; Imakaev, Maxim; Ragoczy, Tobias; Telling, Agnes; Amit, Ido; Lajoie, Bryan R.; Sabo, Peter J.; Dorschner, Michael O.; Sandstrom, Richard; Bernstein, Bradley; Bender, M. A.; Groudine, Mark; Gnirke, Andreas (2009-10-09). "Comprehensive Mapping of Long-Range Interactions Reveals Folding Principles of the Human Genome". Science. 326 (5950): 289–293. Bibcode:2009Sci...326..289L. doi:10.1126/science.1181369. PMC   2858594 . PMID   19815776.
61. Hsieh, Tsung-Han S.; Fudenberg, Geoffrey; Goloborodko, Anton; Rando, Oliver J. (December 2016). "Micro-C XL: assaying chromosome conformation from the nucleosome to the entire genome". Nature Methods. 13 (12): 1009–1011. doi:10.1038/nmeth.4025. PMID   27723753.
62. Krietenstein, Nils; Abraham, Sameer; Venev, Sergey V.; Abdennur, Nezar; Gibcus, Johan; Hsieh, Tsung-Han S.; Parsi, Krishna Mohan; Yang, Liyan; Maehr, René; Mirny, Leonid A.; Dekker, Job; Rando, Oliver J. (May 2020). "Ultrastructural Details of Mammalian Chromosome Architecture". Molecular Cell. 78 (3): 554–565.e7. doi:10.1016/j.molcel.2020.03.003. PMC   7222625 . PMID   32213324.
63. Rao, Suhas S.P.; Huang, Su-Chen; Glenn St Hilaire, Brian; Engreitz, Jesse M.; Perez, Elizabeth M.; Kieffer-Kwon, Kyong-Rim; Sanborn, Adrian L.; Johnstone, Sarah E.; Bascom, Gavin D.; Bochkov, Ivan D.; Huang, Xingfan; Shamim, Muhammad S.; Shin, Jaeweon; Turner, Douglass; Ye, Ziyi (October 2017). "Cohesin Loss Eliminates All Loop Domains". Cell. 171 (2): 305–320.e24. doi:10.1016/j.cell.2017.09.026. PMC   5846482 . PMID   28985562.
64. Wendt, Kerstin S.; Peters, Jan-Michael (February 2009). "How cohesin and CTCF cooperate in regulating gene expression". Chromosome Research. 17 (2): 201–214. doi:10.1007/s10577-008-9017-7. PMID   19308701.
65. Mach, Pia; Kos, Pavel I.; Zhan, Yinxiu; Cramard, Julie; Gaudin, Simon; Tünnermann, Jana; Marchi, Edoardo; Eglinger, Jan; Zuin, Jessica; Kryzhanovska, Mariya; Smallwood, Sebastien; Gelman, Laurent; Roth, Gregory; Nora, Elphège P.; Tiana, Guido (December 2022). "Cohesin and CTCF control the dynamics of chromosome folding". Nature Genetics. 54 (12): 1907–1918. doi:10.1038/s41588-022-01232-7. PMC   9729113 . PMID   36471076.
66. Gabriele, Michele; Brandão, Hugo B.; Grosse-Holz, Simon; Jha, Asmita; Dailey, Gina M.; Cattoglio, Claudia; Hsieh, Tsung-Han S.; Mirny, Leonid; Zechner, Christoph; Hansen, Anders S. (2022-04-29). "Dynamics of CTCF- and cohesin-mediated chromatin looping revealed by live-cell imaging". Science. 376 (6592): 496–501. Bibcode:2022Sci...376..496G. doi:10.1126/science.abn6583. PMC   9069445 . PMID   35420890.
67. van Staalduinen, Jente; van Staveren, Thomas; Grosveld, Frank; Wendt, Kerstin S. (2023-06-23). "Live-cell imaging of chromatin contacts opens a new window into chromatin dynamics". Epigenetics & Chromatin. 16 (1): 27. doi: 10.1186/s13072-023-00503-9 . PMC   10288748 . PMID   37349773.
68. Gard S, Light W, Xiong B, Bose T, McNairn AJ, Harris B, Fleharty B, Seidel C, Brickner JH, Gerton JL (November 2009). "Cohesinopathy mutations disrupt the subnuclear organization of chromatin". The Journal of Cell Biology. 187 (4): 455–62. doi:10.1083/jcb.200906075. PMC   2779225 . PMID   19948494.
69. van der Lelij P, Chrzanowska KH, Godthelp BC, Rooimans MA, Oostra AB, Stumm M, Zdzienicka MZ, Joenje H, de Winter JP (February 2010). "Warsaw breakage syndrome, a cohesinopathy associated with mutations in the XPD helicase family member DDX11/ChlR1". American Journal of Human Genetics. 86 (2): 262–6. doi:10.1016/j.ajhg.2010.01.008. PMC   2820174 . PMID   20137776.
70. van der Lelij P, Godthelp BC, van Zon W, van Gosliga D, Oostra AB, Steltenpool J, de Groot J, Scheper RJ, Wolthuis RM, Waisfisz Q, Darroudi F, Joenje H, de Winter JP (September 2009). Warburton PE (ed.). "The cellular phenotype of Roberts syndrome fibroblasts as revealed by ectopic expression of ESCO2". PLOS ONE. 4 (9): e6936. Bibcode:2009PLoSO...4.6936V. doi: 10.1371/journal.pone.0006936 . PMC   2734174 . PMID   19738907.
71. Kaur, Maninder; Blair, Justin; Devkota, Batsal; Fortunato, Sierra; Clark, Dinah; Lawrence, Audrey; Kim, Jiwoo; Do, Wonwook; Semeo, Benjamin; Katz, Olivia; Mehta, Devanshi; Yamamoto, Nobuko; Schindler, Emma; Al Rawi, Zayd; Wallace, Nina (August 2023). "Genomic analyses in Cornelia de Lange Syndrome and related diagnoses: Novel candidate genes, genotype–phenotype correlations and common mechanisms". American Journal of Medical Genetics Part A. 191 (8): 2113–2131. doi:10.1002/ajmg.a.63247. PMC   10524367 . PMID   37377026.
72. Vega, Hugo; Waisfisz, Quinten; Gordillo, Miriam; Sakai, Norio; Yanagihara, Itaru; Yamada, Minoru; van Gosliga, Djoke; Kayserili, Hülya; Xu, Chengzhe; Ozono, Keiichi; Wang Jabs, Ethylin; Inui, Koji; Joenje, Hans (May 2005). "Roberts syndrome is caused by mutations in ESCO2, a human homolog of yeast ECO1 that is essential for the establishment of sister chromatid cohesion". Nature Genetics. 37 (5): 468–470. doi:10.1038/ng1548. PMID   15821733.
73. van der Lelij, Petra; Chrzanowska, Krystyna H.; Godthelp, Barbara C.; Rooimans, Martin A.; Oostra, Anneke B.; Stumm, Markus; Zdzienicka, Małgorzata Z.; Joenje, Hans; de Winter, Johan P. (February 2010). "Warsaw Breakage Syndrome, a Cohesinopathy Associated with Mutations in the XPD Helicase Family Member DDX11/ChlR1". The American Journal of Human Genetics. 86 (2): 262–266. doi:10.1016/j.ajhg.2010.01.008. PMC   2820174 . PMID   20137776.
74. De Koninck, Magali; Losada, Ana (December 2016). "Cohesin Mutations in Cancer". Cold Spring Harbor Perspectives in Medicine. 6 (12): a026476. doi:10.1101/cshperspect.a026476. PMC   5131750 . PMID   27742736.
75. Waldman, Todd (September 2020). "Emerging themes in cohesin cancer biology". Nature Reviews Cancer. 20 (9): 504–515. doi:10.1038/s41568-020-0270-1. PMID   32514055.
76. Tothova, Zuzana; Valton, Anne-Laure; Gorelov, Rebecca A.; Vallurupalli, Mounica; Krill-Burger, John M.; Holmes, Amie; Landers, Catherine C.; Haydu, J. Erika; Malolepsza, Edyta; Hartigan, Christina; Donahue, Melanie; Popova, Katerina D.; Koochaki, Sebastian; Venev, Sergey V.; Rivera, Jeanne (2021-02-08). "Cohesin mutations alter DNA damage repair and chromatin structure and create therapeutic vulnerabilities in MDS/AML". JCI Insight. 6 (3). doi:10.1172/jci.insight.142149. PMC   7934867 . PMID   33351783.
77. Viny, Aaron D.; Bowman, Robert L.; Liu, Yu; Lavallée, Vincent-Philippe; Eisman, Shira E.; Xiao, Wenbin; Durham, Benjamin H.; Navitski, Anastasia; Park, Jane; Braunstein, Stephanie; Alija, Besmira; Karzai, Abdul; Csete, Isabelle S.; Witkin, Matthew; Azizi, Elham (November 2019). "Cohesin Members Stag1 and Stag2 Display Distinct Roles in Chromatin Accessibility and Topological Control of HSC Self-Renewal and Differentiation". Cell Stem Cell. 25 (5): 682–696.e8. doi:10.1016/j.stem.2019.08.003. PMC   6842438 . PMID   31495782.

Further reading

• Mehta GD, Rizvi SM, Ghosh SK (August 2012). "Cohesin: a guardian of genome integrity". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1823 (8): 1324–42. doi: 10.1016/j.bbamcr.2012.05.027 . PMID   22677545.
• Mehta GD, Kumar R, Srivastava S, Ghosh SK (August 2013). "Cohesin: functions beyond sister chromatid cohesion". FEBS Letters. 587 (15): 2299–312. Bibcode:2013FEBSL.587.2299M. doi:10.1016/j.febslet.2013.06.035. PMID   23831059. S2CID   39397443.
• Michaelis C, Ciosk R, Nasmyth K (October 1997). "Cohesins: chromosomal proteins that prevent premature separation of sister chromatids". Cell. 91 (1): 35–45. doi: 10.1016/S0092-8674(01)80007-6 . PMID   9335333.
• Guacci V, Koshland D, Strunnikov A (October 1997). "A direct link between sister chromatid cohesion and chromosome condensation revealed through the analysis of MCD1 in S. cerevisiae". Cell. 91 (1): 47–57. doi:10.1016/S0092-8674(01)80008-8. PMC   2670185 . PMID   9335334.
• Tóth A, Ciosk R, Uhlmann F, Galova M, Schleiffer A, Nasmyth K (February 1999). "Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to establish cohesion between sister chromatids during DNA replication". Genes & Development. 13 (3): 320–33. doi:10.1101/gad.13.3.320. PMC   316435 . PMID   9990856.
• Uhlmann F, Lottspeich F, Nasmyth K (July 1999). "Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1". Nature. 400 (6739): 37–42. Bibcode:1999Natur.400...37U. doi:10.1038/21831. PMID   10403247. S2CID   4354549.

External links

• Media related to Cohesins at Wikimedia Commons
• cohesin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)