SWI/SNF

Last updated • 6 min readFrom Wikipedia, The Free Encyclopedia
Snf2 ATPase bound to a nucleosome
Snf2 ATPase domain in complex with a nucleosome.png
Cryo-EM reconstruction of S. cerevisiae Snf2 ATPase in complex with a nucleosome
Identifiers
SymbolSnf2
Pfam PF00176
InterPro IPR000330
SMART DEXDc
SCOP2 5x0x / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In molecular biology, SWI/SNF (SWItch/Sucrose Non-Fermentable), [1] [2] is a subfamily of ATP-dependent chromatin remodeling complexes, which is found in eukaryotes. In other words, it is a group of proteins that associate to remodel the way DNA is packaged. This complex is composed of several proteins – products of the SWI and SNF genes ( SWI1 , SWI2 / SNF2 , SWI3 , SWI5 , SWI6 ), as well as other polypeptides. [3] It possesses a DNA-stimulated ATPase activity that can destabilize histone-DNA interactions in reconstituted nucleosomes in an ATP-dependent manner, though the exact nature of this structural change is unknown. The SWI/SNF subfamily provides crucial nucleosome rearrangement, which is seen as ejection and/or sliding. The movement of nucleosomes provides easier access to the chromatin, enabling binding of specific transcription factors, [4] and allowing genes to be activated or repressed. [5]

Contents

The human analogs of SWI/SNF are "BRG1- or BRM-associated factors", or BAF (SWI/SNF-A) and "Polybromo-associated BAF", which is also known as PBAF (SWI/SNF-B). [6] There are also Drosophila analogs of SWI/SNF, known as "Brahma Associated Protein", or BAP and "Polybromo-associated BAP", also known as PBAP. [7]

Mechanism of action

It has been found that the SWI/SNF complex (in yeast) is capable of altering the position of nucleosomes along DNA. [8] [9] These alterations are classified in three different ways, and they are seen as the processes of sliding nucleosomes, ejecting nucleosomes, and ejecting only certain components of the nucleosome. [5] Due to the actions performed by the SWI/SNF subfamily, they are referred to as "access remodellers" and promote gene expression by exposing binding sites so that transcription factors can bind more easily. [5] Two mechanisms for nucleosome remodeling by SWI/SNF have been proposed. [10] The first model contends that a unidirectional diffusion of a twist defect within the nucleosomal DNA results in a corkscrew-like propagation of DNA over the octamer surface that initiates at the DNA entry site of the nucleosome. The other is known as the "bulge" or "loop-recapture" mechanism and it involves the dissociation of DNA at the edge of the nucleosome with re-association of DNA inside the nucleosome, forming a DNA bulge on the octamer surface. The DNA loop would then propagate across the surface of the histone octamer in a wave-like manner, resulting in the re-positioning of DNA without changes in the total number of histone-DNA contacts. [11] A recent study [12] has provided strong evidence against the twist diffusion mechanism and has further strengthened the loop-recapture model.

Role as a tumor suppressor

The mammalian SWI/SNF (mSWI/SNF) complex functions as a tumor suppressor in many human malignant cancers. [13] Early studies identified that SWI/SNF subunits were frequently absent in cancer cell lines. [14] SWI/SNF was first identified in 1998 as a tumor suppressor in rhabdoid tumors, a rare pediatric malignant cancer. [15] Other instances of SWI/SNF acting as a tumor suppressor comes from the heterozygous deletion of BAF47 [16] or alteration of BAF47. [17] These instances result in cases of chronic and acute CML and in rarer cases, Hodgkin's lymphoma, respectively. To prove that BAF47, also known as SMARCB1, acts as a tumor suppressor, experiments resulting in the formation of rhabdoid tumors in mice were conducted via total knockout of BAF47. [18] As DNA sequencing costs diminished, many tumors were sequenced for the first time around 2010. Several of these studies revealed SWI/SNF to be a tumor suppressor in a number of diverse malignancies. [19] [20] [21] [22] Several studies revealed that subunits of the mammalian complex, including ARID1A, [23] PBRM1, [22] SMARCB1, [24] SMARCA4, [25] and ARID2, [20] are frequently mutated in human cancers. It has been noted that total loss of BAF47 is extremely rare and instead, most cases of tumors that resulted from SWI/SNF subunits come from BRG1 deletion, BRM deletion, or total loss of both subunits. [26] Further analysis concluded that total loss of both subunits was present in about 10% of tumor cell lines after 100 cell lines were looked at. [27] A meta-analysis of many sequencing studies demonstrated SWI/SNF to be mutated in approximately 20% of human malignancies. [28]

Role as a cancer dependency

The function of the mammalian SWI/SNF complex is highly tissue-specific, [29] and in addition to its role as a tumor suppressor described above, SWI/SNF complexes also act as dependencies in several different cancer contexts, including acute myeloid leukemia, [30] [31] prostate cancer, [32] neuroblastoma, [33] uveal melanoma, [34] synovial sarcoma, [35] and lung cancer. [36] Because SWI/SNF complexes are viewed as potentially viable drug targets for treating tumors that depend of SWI/SNF activity, [37] several programs in the pharmaceutical industry [38] [39] [40] and in academic settings [41] [32] have sought to develop inhibitors or protein degraders of the complex. Small molecules that inactivate SWI/SNF complexes by interfering with ATP hydrolysis [30] [38] or by causing degradation of key protein subunits [39] have demonstrated efficacy in pre-clinical studies. Common to many of these settings is the requirement of SWI/SNF activity to promote the expression of genes involved in replication commitment, specifically for the expression of proteins that promote transition between G1 and S phase of the cell cycle. [33] This area is rapidly evolving and the development of drugs targeting these complexes is ongoing.

Structure of the SWI/SNF complex

Domain organization of SWI/SNF: a subfamily within the ATP-Dependent chromatin remodeling complexes Sniff2.jpg
Domain organization of SWI/SNF: a subfamily within the ATP-Dependent chromatin remodeling complexes

Electron microscopy studies of SWI/SNF and RSC (SWI/SNF-B) reveal large, lobed 1.1-1.3 MDa structures. [42] [43] [44] [45] These structures resemble RecA and cover both sides of a conserved section of the ATPase domain. The domain also contains a separate domain, HSA, that is capable of binding actin, and resides on the N-terminus. [5] The bromo domain present is responsible for recognizing and binding lysines that have been acetylated. [7] No atomic-resolution structures of the entire SWI/SNF complex have been obtained to date, due to the protein complex being highly dynamic and composed of many subunits. However, domains and several individual subunits from yeast and mammals have been described. In particular, the cryo-EM structure of the ATPase Snf2 in complex with a nucleosome shows that nucleosomal DNA is locally deformed at the site of binding. [46] A model of the mammalian ATPase SMARCA4 shows similar features, [25] based on the high degree of sequence homology with yeast Snf2. The interface between two subunits, BAF155 (SMARCC1) and BAF47 (SMARCB1) was also resolved, providing important insights into the mechanisms of the SWI/SNF complex assembly pathway. [47]

SWIB/MDM2 protein domain

The protein domain, SWIB/MDM2, short for SWI/SNF complex B/MDM2 is an important domain. This protein domain has been found in both SWI/SNF complex B and in the negative regulator of the p53 tumor suppressor MDM2. It has been shown that MDM2 is homologous to the SWIB complex. [48]

Function

The primary function of the SWIB protein domain is to aid gene expression. In yeast, this protein domain expresses certain genes, in particular BADH2, GAL1, GAL4, and SUC2. It works by increasing transcription. It has ATPase activity, meaning it breaks down ATP, the basic unit of energy currency. This destabilizes the interaction between DNA and histones. The destabilization that occurs disrupts chromatin and opens up the transcription-binding domains. Transcription factors can then bind to this site, leading to an increase in transcription. [49]

Protein interaction

The various protein subunits that make up the SWI/SNF complex interact with each other in different configurations to form three distinct types of SWI/SNF complex: canonical BAF (cBAF), polybromo-associated BAF (pBAF) and non-canonical BAF (ncBAF). Specifically, cBAF is currently thought to regulate gene enhancers, while pBAF and ncBAF function at regions proximal to gene promoters. [50] In addition to their many interactions within the family of SWI/SNF related proteins, some subunits such as SNF5 and BAF155 are capable of interacting with transcription factors, such as c-MYC and the FOS and JUN family proteins of the AP-1 complex. [51] [52]

Structure

This protein domain is known to contain one short alpha helix.

Family members

Below is a list of yeast SWI/SNF family members with human and Drosophila [53] orthologs: [54]

YeastHumanDrosophilaFunction
SWI1 ARID1A, ARID1B OSA Contains LXXLL nuclear receptor binding motifs
SWI2 / SNF2 SMARCA2, SMARCA4 BRM ATP dependent chromatin remodeling
SWI3 SMARCC1, SMARCC2 Moira/BAP155 Similar sequence; function unknown
SWP73 /SNF12 SMARCD1, SMARCD2, SMARCD3 BAP60 Similar sequence; function unknown
SWP61 /ARP7 ACTL6A, ACTL6B Actin-like protein
SNF5 SMARCB1 SNR1 ATP dependent chromatin remodeling

History

The SWI/SNF complex was first discovered in the yeast, Saccharomyces cerevisiae . It was named after initially screening for mutations that would affect the pathways for both yeast mating types switching (SWI) and sucrose non-fermenting (SNF). [49] [7]

See also

Related Research Articles

<span class="mw-page-title-main">Nucleosome</span> Basic structural unit of DNA packaging in eukaryotes

A nucleosome is the basic structural unit of DNA packaging in eukaryotes. The structure of a nucleosome consists of a segment of DNA wound around eight histone proteins and resembles thread wrapped around a spool. The nucleosome is the fundamental subunit of chromatin. Each nucleosome is composed of a little less than two turns of DNA wrapped around a set of eight proteins called histones, which are known as a histone octamer. Each histone octamer is composed of two copies each of the histone proteins H2A, H2B, H3, and H4.

RSC is a member of the ATP-dependent chromatin remodeler family. The activity of the RSC complex allows for chromatin to be remodeled by altering the structure of the nucleosome.

Chromatin remodeling is the dynamic modification of chromatin architecture to allow access of condensed genomic DNA to the regulatory transcription machinery proteins, and thereby control gene expression. Such remodeling is principally carried out by 1) covalent histone modifications by specific enzymes, e.g., histone acetyltransferases (HATs), deacetylases, methyltransferases, and kinases, and 2) ATP-dependent chromatin remodeling complexes which either move, eject or restructure nucleosomes. Besides actively regulating gene expression, dynamic remodeling of chromatin imparts an epigenetic regulatory role in several key biological processes, egg cells DNA replication and repair; apoptosis; chromosome segregation as well as development and pluripotency. Aberrations in chromatin remodeling proteins are found to be associated with human diseases, including cancer. Targeting chromatin remodeling pathways is currently evolving as a major therapeutic strategy in the treatment of several cancers.

<span class="mw-page-title-main">SMARCA4</span> Protein-coding gene in the species Homo sapiens

Transcription activator BRG1 also known as ATP-dependent chromatin remodeler SMARCA4 is a protein that in humans is encoded by the SMARCA4 gene.

<span class="mw-page-title-main">SMARCB1</span> Protein-coding gene in the species Homo sapiens

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 is a protein that in humans is encoded by the SMARCB1 gene.

<span class="mw-page-title-main">SMARCA2</span> Protein-coding gene in the species Homo sapiens

Probable global transcription activator SNF2L2 is a protein that in humans is encoded by the SMARCA2 gene.

<span class="mw-page-title-main">ACTL6A</span> Protein-coding gene in the species Homo sapiens

Actin-like protein 6A is a protein that in humans is encoded by the ACTL6A gene.

<span class="mw-page-title-main">ARID1A</span> Protein-coding gene in humans

AT-rich interactive domain-containing protein 1A is a protein that in humans is encoded by the ARID1A gene.

<span class="mw-page-title-main">SMARCC1</span> Protein-coding gene in the species Homo sapiens

SWI/SNF complex subunit SMARCC1 is a protein that in humans is encoded by the SMARCC1 gene.

<span class="mw-page-title-main">SMARCE1</span> Protein-coding gene in the species Homo sapiens

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 is a protein that in humans is encoded by the SMARCE1 gene.

<span class="mw-page-title-main">ARID1B</span> Protein-coding gene in humans

AT-rich interactive domain-containing protein 1B is a protein that in humans is encoded by the ARID1B gene. ARID1B is a component of the human SWI/SNF chromatin remodeling complex.

<span class="mw-page-title-main">SMARCD1</span> Protein-coding gene in the species Homo sapiens

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1 is a protein that in humans is encoded by the SMARCD1 gene.

<span class="mw-page-title-main">CHD1</span> Chromatin remodeling protein that is widely conserved across many eukaryotic organisms

The Chromodomain-Helicase DNA-binding 1 is a protein that, in humans, is encoded by the CHD1 gene. CHD1 is a chromatin remodeling protein that is widely conserved across many eukaryotic organisms, from yeast to humans. CHD1 is named for three of its protein domains: two tandem chromodomains, its ATPase catalytic domain, and its DNA-binding domain.

<span class="mw-page-title-main">PBRM1</span> Protein-coding gene in the species Homo sapiens

Protein polybromo-1 (PB1) also known as BRG1-associated factor 180 (BAF180) is a protein that in humans is encoded by the PBRM1 gene.

<span class="mw-page-title-main">SMARCD2</span> Protein-coding gene in the species Homo sapiens

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2 is a protein that in humans is encoded by the SMARCD2 gene.

ISWI is one of the five major DNA chromatin remodeling complex types, or subfamilies, found in most eukaryotic organisms. ISWI remodeling complexes place nucleosomes along segments of DNA at regular intervals. The placement of nucleosomes by ISWI protein complexes typically results in the silencing of the DNA because the nucleosome placement prevents transcription of the DNA. ISWI, like the closely related SWI/SNF subfamily, is an ATP-dependent chromatin remodeler. However, the chromatin remodeling activities of ISWI and SWI/SNF are distinct and mediate the binding of non-overlapping sets of DNA transcription factors.

In the field of molecular biology, the Mi-2/NuRDcomplex, is a group of associated proteins with both ATP-dependent chromatin remodeling and histone deacetylase activities. As of 2007, Mi-2/NuRD was the only known protein complex that couples chromatin remodeling ATPase and chromatin deacetylation enzymatic functions.

<span class="mw-page-title-main">Diana Hargreaves</span> American biologist

Diana Hargreaves is an American biologist and assistant professor at The Salk Institute for Biological Studies and member of The Salk Cancer Center. Her laboratory focuses on epigenetic regulation by the BAF (SWI/SNF) chromatin remodeling complexes in diverse physiological processes including development, immunity, and diseases such as cancer.

Robert E. Kingston is an American biochemist and geneticist who studies the functional and regulatory role nucleosomes play in gene expression, specifically during early development. After receiving his PhD (1981) and completing post-doctoral research, Kingston became an assistant professor at Massachusetts General Hospital (1985), where he started a research laboratory focused on understanding chromatin's structure with regards to transcriptional regulation. As a Harvard graduate himself, Kingston has served his alma mater through his leadership.

Cigall Kadoch is an American biochemist and cancer biologist who is Associate Professor of Pediatric Oncology at the Dana–Farber Cancer Institute and Harvard Medical School and an Investigator at the Howard Hughes Medical Institute. Her research is focused in chromatin regulation and how changes in cellular structure can lead to human diseases, such as Cancer, Neurodevelopmental disorders, and others. She is internationally recognized for her work on the mammalian SWI/SNF complex, a large molecular machine known as a Chromatin remodeling complex. She was named as one of the world's leading scientists by MIT Technology Review, 35 Under 35 and Forbes 30 Under 30, and a Finalist for the Blavatnik Awards for Young Scientists. In 2019, she received the Martin and Rose Wachtel Cancer Research Prize from the American Association for the Advancement of Science and in 2020, the American Association for Cancer Research Outstanding Achievement in Basic Cancer Research Award. Kadoch was also recognized as one of the 100 Influential Women in Oncology by OncoDaily.

References

  1. ↑ Neigeborn L, Carlson M (December 1984). "Genes affecting the regulation of SUC2 gene expression by glucose repression in Saccharomyces cerevisiae". Genetics. 108 (4): 845–858. doi:10.1093/genetics/108.4.845. PMC   1224269 . PMID   6392017.
  2. ↑ Stern M, Jensen R, Herskowitz I (October 1984). "Five SWI genes are required for expression of the HO gene in yeast". Journal of Molecular Biology. 178 (4): 853–868. doi:10.1016/0022-2836(84)90315-2. PMID   6436497.
  3. ↑ Pazin MJ, Kadonaga JT (March 1997). "SWI2/SNF2 and related proteins: ATP-driven motors that disrupt protein-DNA interactions?". Cell. 88 (6): 737–740. doi: 10.1016/S0092-8674(00)81918-2 . PMID   9118215.
  4. ↑ Barisic, Darko; Stadler, Michael B.; Iurlaro, Mario; Schübeler, Dirk (May 2019). "Mammalian ISWI and SWI/SNF selectively mediate binding of distinct transcription factors". Nature. 569 (7754): 136–140. Bibcode:2019Natur.569..136B. doi:10.1038/s41586-019-1115-5. ISSN   1476-4687. PMC   6522387 . PMID   30996347.
  5. 1 2 3 4 Clapier CR, Iwasa J, Cairns BR, Peterson CL (July 2017). "Mechanisms of action and regulation of ATP-dependent chromatin-remodelling complexes". Nature Reviews. Molecular Cell Biology. 18 (7): 407–422. doi:10.1038/nrm.2017.26. PMC   8127953 . PMID   28512350.
  6. ↑ Nie Z, Yan Z, Chen EH, Sechi S, Ling C, Zhou S, et al. (April 2003). "Novel SWI/SNF chromatin-remodeling complexes contain a mixed-lineage leukemia chromosomal translocation partner". Molecular and Cellular Biology. 23 (8): 2942–2952. doi:10.1128/MCB.23.8.2942-2952.2003. PMC   152562 . PMID   12665591.
  7. 1 2 3 Tang L, Nogales E, Ciferri C (June 2010). "Structure and function of SWI/SNF chromatin remodeling complexes and mechanistic implications for transcription". Progress in Biophysics and Molecular Biology. 102 (2–3): 122–128. doi:10.1016/j.pbiomolbio.2010.05.001. PMC   2924208 . PMID   20493208.
  8. ↑ Hirschhorn JN, Brown SA, Clark CD, Winston F (December 1992). "Evidence that SNF2/SWI2 and SNF5 activate transcription in yeast by altering chromatin structure". Genes & Development. 6 (12A): 2288–2298. doi: 10.1101/gad.6.12a.2288 . PMID   1459453.
  9. ↑ Whitehouse I, Flaus A, Cairns BR, White MF, Workman JL, Owen-Hughes T (August 1999). "Nucleosome mobilization catalysed by the yeast SWI/SNF complex". Nature. 400 (6746): 784–787. Bibcode:1999Natur.400..784W. doi:10.1038/23506. PMID   10466730. S2CID   2841873.
  10. ↑ van Holde K, Yager T (June 2003). "Models for chromatin remodeling: a critical comparison". Biochemistry and Cell Biology. 81 (3): 169–172. doi:10.1139/o03-038. PMID   12897850.
  11. ↑ Flaus A, Owen-Hughes T (April 2003). "Mechanisms for nucleosome mobilization". Biopolymers. 68 (4): 563–578. doi:10.1002/bip.10323. PMID   12666181.
  12. ↑ Zofall M, Persinger J, Kassabov SR, Bartholomew B (April 2006). "Chromatin remodeling by ISW2 and SWI/SNF requires DNA translocation inside the nucleosome". Nature Structural & Molecular Biology. 13 (4): 339–346. doi:10.1038/nsmb1071. PMID   16518397. S2CID   24163324.
  13. ↑ Hodges C, Kirkland JG, Crabtree GR (August 2016). "The Many Roles of BAF (mSWI/SNF) and PBAF Complexes in Cancer". Cold Spring Harbor Perspectives in Medicine. 6 (8): a026930. doi:10.1101/cshperspect.a026930. PMC   4968166 . PMID   27413115.
  14. ↑ Dunaief JL, Strober BE, Guha S, Khavari PA, Alin K, Luban J, et al. (October 1994). "The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest". Cell. 79 (1): 119–130. doi:10.1016/0092-8674(94)90405-7. PMID   7923370. S2CID   7058539.
  15. ↑ Versteege I, Sévenet N, Lange J, Rousseau-Merck MF, Ambros P, Handgretinger R, et al. (July 1998). "Truncating mutations of hSNF5/INI1 in aggressive paediatric cancer". Nature. 394 (6689): 203–206. Bibcode:1998Natur.394..203V. doi:10.1038/28212. PMID   9671307. S2CID   6019090.
  16. ↑ Melo JV, Gordon DE, Cross NC, Goldman JM (January 1993). "The ABL-BCR fusion gene is expressed in chronic myeloid leukemia". Blood. 81 (1): 158–165. doi: 10.1182/blood.v81.1.158.bloodjournal811158 . PMID   8417787.
  17. ↑ Yuge M, Nagai H, Uchida T, Murate T, Hayashi Y, Hotta T, et al. (October 2000). "HSNF5/INI1 gene mutations in lymphoid malignancy". Cancer Genetics and Cytogenetics. 122 (1): 37–42. doi:10.1016/s0165-4608(00)00274-0. PMID   11104031.
  18. ↑ Reisman D, Glaros S, Thompson EA (April 2009). "The SWI/SNF complex and cancer". Oncogene. 28 (14): 1653–1668. doi:10.1038/onc.2009.4. PMID   19234488.
  19. ↑ Wiegand KC, Shah SP, Al-Agha OM, Zhao Y, Tse K, Zeng T, et al. (October 2010). "ARID1A mutations in endometriosis-associated ovarian carcinomas". The New England Journal of Medicine. 363 (16): 1532–1543. doi:10.1056/NEJMoa1008433. PMC   2976679 . PMID   20942669.
  20. 1 2 Li M, Zhao H, Zhang X, Wood LD, Anders RA, Choti MA, et al. (August 2011). "Inactivating mutations of the chromatin remodeling gene ARID2 in hepatocellular carcinoma". Nature Genetics. 43 (9): 828–829. doi:10.1038/ng.903. PMC   3163746 . PMID   21822264.
  21. ↑ Shain AH, Giacomini CP, Matsukuma K, Karikari CA, Bashyam MD, Hidalgo M, et al. (January 2012). "Convergent structural alterations define SWItch/Sucrose NonFermentable (SWI/SNF) chromatin remodeler as a central tumor suppressive complex in pancreatic cancer". Proceedings of the National Academy of Sciences of the United States of America. 109 (5): E252–E259. doi: 10.1073/pnas.1114817109 . PMC   3277150 . PMID   22233809.
  22. 1 2 Varela I, Tarpey P, Raine K, Huang D, Ong CK, Stephens P, et al. (January 2011). "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma". Nature. 469 (7331): 539–542. Bibcode:2011Natur.469..539V. doi:10.1038/nature09639. PMC   3030920 . PMID   21248752.
  23. ↑ Mathur R, Alver BH, San Roman AK, Wilson BG, Wang X, Agoston AT, et al. (February 2017). "ARID1A loss impairs enhancer-mediated gene regulation and drives colon cancer in mice". Nature Genetics. 49 (2): 296–302. doi:10.1038/ng.3744. PMC   5285448 . PMID   27941798.
  24. ↑ Isakoff MS, Sansam CG, Tamayo P, Subramanian A, Evans JA, Fillmore CM, et al. (December 2005). "Inactivation of the Snf5 tumor suppressor stimulates cell cycle progression and cooperates with p53 loss in oncogenic transformation". Proceedings of the National Academy of Sciences of the United States of America. 102 (49): 17745–17750. Bibcode:2005PNAS..10217745I. doi: 10.1073/pnas.0509014102 . PMC   1308926 . PMID   16301525.
  25. 1 2 Hodges HC, Stanton BZ, Cermakova K, Chang CY, Miller EL, Kirkland JG, et al. (January 2018). "Dominant-negative SMARCA4 mutants alter the accessibility landscape of tissue-unrestricted enhancers". Nature Structural & Molecular Biology. 25 (1): 61–72. doi:10.1038/s41594-017-0007-3. PMC   5909405 . PMID   29323272.
  26. ↑ Muchardt C, Yaniv M (May 2001). "When the SWI/SNF complex remodels...the cell cycle". Oncogene. 20 (24): 3067–3075. doi:10.1038/sj.onc.1204331. PMID   11420722.
  27. ↑ Decristofaro MF, Betz BL, Rorie CJ, Reisman DN, Wang W, Weissman BE (January 2001). "Characterization of SWI/SNF protein expression in human breast cancer cell lines and other malignancies". Journal of Cellular Physiology. 186 (1): 136–145. doi:10.1002/1097-4652(200101)186:1<136::aid-jcp1010>3.0.co;2-4. PMID   11147808. S2CID   25016283.
  28. ↑ Shain AH, Pollack JR (2013). "The spectrum of SWI/SNF mutations, ubiquitous in human cancers". PLOS ONE. 8 (1): e55119. Bibcode:2013PLoSO...855119S. doi: 10.1371/journal.pone.0055119 . PMC   3552954 . PMID   23355908.
  29. ↑ Alver, Burak H.; Kim, Kimberly H.; Lu, Ping; Wang, Xiaofeng; Manchester, Haley E.; Wang, Weishan; Haswell, Jeffrey R.; Park, Peter J.; Roberts, Charles W. M. (2017-03-06). "The SWI/SNF chromatin remodelling complex is required for maintenance of lineage specific enhancers". Nature Communications. 8: 14648. Bibcode:2017NatCo...814648A. doi:10.1038/ncomms14648. ISSN   2041-1723. PMC   5343482 . PMID   28262751.
  30. 1 2 Chambers, Courtney; Cermakova, Katerina; Chan, Yuen San; Kurtz, Kristen; Wohlan, Katharina; Lewis, Andrew Henry; Wang, Christiana; Pham, Anh; Dejmek, Milan; Sala, Michal; Loeza Cabrera, Mario; Aguilar, Rogelio; Nencka, Radim; Lacorazza, Daniel; Rau, Rachel E. (2023-01-20). "SWI/SNF blockade disrupts PU.1-directed enhancer programs in normal hematopoietic cells and acute myeloid leukemia". Cancer Research. 83 (7): CAN–22–2129. doi:10.1158/0008-5472.CAN-22-2129. ISSN   1538-7445. PMC   10071820 . PMID   36662812. S2CID   256031128.
  31. ↑ Rago, Florencia; Rodrigues, Lindsey Ulkus; Bonney, Megan; Sprouffske, Kathleen; Kurth, Esther; Elliott, GiNell; Ambrose, Jessi; Aspesi, Peter; Oborski, Justin; Chen, Julie T.; McDonald, E. Robert; Mapa, Felipa A.; Ruddy, David A.; Kauffmann, Audrey; Abrams, Tinya (2022-03-01). "Exquisite Sensitivity to Dual BRG1/BRM ATPase Inhibitors Reveals Broad SWI/SNF Dependencies in Acute Myeloid Leukemia". Molecular Cancer Research. 20 (3): 361–372. doi: 10.1158/1541-7786.MCR-21-0390 . ISSN   1557-3125. PMID   34799403. S2CID   244454472.
  32. 1 2 Xiao, Lanbo; Parolia, Abhijit; Qiao, Yuanyuan; Bawa, Pushpinder; Eyunni, Sanjana; Mannan, Rahul; Carson, Sandra E.; Chang, Yu; Wang, Xiaoju; Zhang, Yuping; Vo, Josh N.; Kregel, Steven; Simko, Stephanie A.; Delekta, Andrew D.; Jaber, Mustapha (January 2022). "Targeting SWI/SNF ATPases in enhancer-addicted prostate cancer". Nature. 601 (7893): 434–439. Bibcode:2022Natur.601..434X. doi:10.1038/s41586-021-04246-z. ISSN   1476-4687. PMC   8770127 . PMID   34937944.
  33. 1 2 Cermakova, Katerina; Tao, Ling; Dejmek, Milan; Sala, Michal; Montierth, Matthew D.; Chan, Yuen San; Patel, Ivanshi; Chambers, Courtney; Loeza Cabrera, Mario; Hoffman, Dane; Parchem, Ronald J.; Wang, Wenyi; Nencka, Radim; Barbieri, Eveline; Hodges, H. Courtney (2023-11-23). "Reactivation of the G1 enhancer landscape underlies core circuitry addiction to SWI/SNF". Nucleic Acids Research. 52 (1): 4–21. doi: 10.1093/nar/gkad1081 . ISSN   1362-4962. PMC   10783513 . PMID   37993417.
  34. ↑ Rago, Florencia; Elliott, GiNell; Li, Ailing; Sprouffske, Kathleen; Kerr, Grainne; Desplat, Aurore; Abramowski, Dorothee; Chen, Julie T.; Farsidjani, Ali; Xiang, Kay X.; Bushold, Geoffrey; Feng, Yun; Shirley, Matthew D.; Bric, Anka; Vattay, Anthony (October 2020). "The Discovery of SWI/SNF Chromatin Remodeling Activity as a Novel and Targetable Dependency in Uveal Melanoma". Molecular Cancer Therapeutics. 19 (10): 2186–2195. doi:10.1158/1535-7163.MCT-19-1013. ISSN   1538-8514. PMID   32747420. S2CID   222093985.
  35. ↑ Brien, Gerard L.; Remillard, David; Shi, Junwei; Hemming, Matthew L.; Chabon, Jonathon; Wynne, Kieran; Dillon, Eugène T.; Cagney, Gerard; Van Mierlo, Guido; Baltissen, Marijke P.; Vermeulen, Michiel; Qi, Jun; Fröhling, Stefan; Gray, Nathanael S.; Bradner, James E. (2018-11-15). "Targeted degradation of BRD9 reverses oncogenic gene expression in synovial sarcoma". eLife. 7: e41305. doi: 10.7554/eLife.41305 . ISSN   2050-084X. PMC   6277197 . PMID   30431433.
  36. ↑ Trejo-Villegas, Octavio A.; Irene, Heijink H.; Federico, Ávila-Moreno (2024-06-22). "Preclinical Evidence in the Assembly of Mammalian SWI/SNF Complexes: Epigenetic Insights and Clinical Perspectives in Human Lung Diseases Therapy". Molecular Therapy. doi:10.1016/j.ymthe.2024.06.026. ISSN   1525-0016.
  37. ↑ Hohmann, Anja F.; Vakoc, Christopher R. (August 2014). "A rationale to target the SWI/SNF complex for cancer therapy". Trends in Genetics. 30 (8): 356–363. doi:10.1016/j.tig.2014.05.001. ISSN   0168-9525. PMC   4112150 . PMID   24932742.
  38. 1 2 Papillon, Julien P. N.; Nakajima, Katsumasa; Adair, Christopher D.; Hempel, Jonathan; Jouk, Andriana O.; Karki, Rajeshri G.; Mathieu, Simon; Möbitz, Henrik; Ntaganda, Rukundo; Smith, Troy; Visser, Michael; Hill, Susan E.; Hurtado, Felipe Kellermann; Chenail, Gregg; Bhang, Hyo-Eun C. (2018-11-21). "Discovery of Orally Active Inhibitors of Brahma Homolog (BRM)/SMARCA2 ATPase Activity for the Treatment of Brahma Related Gene 1 (BRG1)/SMARCA4-Mutant Cancers". Journal of Medicinal Chemistry. 61 (22): 10155–10172. doi:10.1021/acs.jmedchem.8b01318. ISSN   1520-4804. PMID   30339381. S2CID   53010943.
  39. 1 2 Cantley, Jennifer; Ye, Xiaofen; Rousseau, Emma; Januario, Tom; Hamman, Brian D.; Rose, Christopher M.; Cheung, Tommy K.; Hinkle, Trent; Soto, Leofal; Quinn, Connor; Harbin, Alicia; Bortolon, Elizabeth; Chen, Xin; Haskell, Roy; Lin, Eva (2022-11-10). "Selective PROTAC-mediated degradation of SMARCA2 is efficacious in SMARCA4 mutant cancers". Nature Communications. 13 (1): 6814. Bibcode:2022NatCo..13.6814C. doi:10.1038/s41467-022-34562-5. ISSN   2041-1723. PMC   9649729 . PMID   36357397.
  40. ↑ Fedorov, Oleg; Castex, Josefina; Tallant, Cynthia; Owen, Dafydd R.; Martin, Sarah; Aldeghi, Matteo; Monteiro, Octovia; Filippakopoulos, Panagis; Picaud, Sarah; Trzupek, John D.; Gerstenberger, Brian S.; Bountra, Chas; Willmann, Dominica; Wells, Christopher; Philpott, Martin (November 2015). "Selective targeting of the BRG/PB1 bromodomains impairs embryonic and trophoblast stem cell maintenance". Science Advances. 1 (10): e1500723. Bibcode:2015SciA....1E0723F. doi:10.1126/sciadv.1500723. ISSN   2375-2548. PMC   4681344 . PMID   26702435.
  41. ↑ Farnaby, William; Koegl, Manfred; Roy, Michael J.; Whitworth, Claire; Diers, Emelyne; Trainor, Nicole; Zollman, David; Steurer, Steffen; Karolyi-Oezguer, Jale; Riedmueller, Carina; Gmaschitz, Teresa; Wachter, Johannes; Dank, Christian; Galant, Michael; Sharps, Bernadette (July 2019). "BAF complex vulnerabilities in cancer demonstrated via structure-based PROTAC design". Nature Chemical Biology. 15 (7): 672–680. doi:10.1038/s41589-019-0294-6. ISSN   1552-4469. PMC   6600871 . PMID   31178587.
  42. ↑ Asturias FJ, Chung WH, Kornberg RD, Lorch Y (October 2002). "Structural analysis of the RSC chromatin-remodeling complex". Proceedings of the National Academy of Sciences of the United States of America. 99 (21): 13477–13480. Bibcode:2002PNAS...9913477A. doi: 10.1073/pnas.162504299 . PMC   129698 . PMID   12368485.
  43. ↑ Leschziner AE, Saha A, Wittmeyer J, Zhang Y, Bustamante C, Cairns BR, Nogales E (March 2007). "Conformational flexibility in the chromatin remodeler RSC observed by electron microscopy and the orthogonal tilt reconstruction method". Proceedings of the National Academy of Sciences of the United States of America. 104 (12): 4913–4918. Bibcode:2007PNAS..104.4913L. doi: 10.1073/pnas.0700706104 . PMC   1820885 . PMID   17360331.
  44. ↑ Smith CL, Horowitz-Scherer R, Flanagan JF, Woodcock CL, Peterson CL (February 2003). "Structural analysis of the yeast SWI/SNF chromatin remodeling complex". Nature Structural Biology. 10 (2): 141–145. doi:10.1038/nsb888. PMID   12524530. S2CID   3140088.
  45. ↑ Chaban Y, Ezeokonkwo C, Chung WH, Zhang F, Kornberg RD, Maier-Davis B, et al. (December 2008). "Structure of a RSC-nucleosome complex and insights into chromatin remodeling". Nature Structural & Molecular Biology. 15 (12): 1272–1277. doi:10.1038/nsmb.1524. PMC   2659406 . PMID   19029894.
  46. ↑ Liu X, Li M, Xia X, Li X, Chen Z (April 2017). "Mechanism of chromatin remodelling revealed by the Snf2-nucleosome structure". Nature. 544 (7651): 440–445. Bibcode:2017Natur.544..440L. doi:10.1038/nature22036. PMID   28424519. S2CID   12392297.
  47. ↑ Yan L, Xie S, Du Y, Qian C (June 2017). "Structural Insights into BAF47 and BAF155 Complex Formation". Journal of Molecular Biology. 429 (11): 1650–1660. doi:10.1016/j.jmb.2017.04.008. PMID   28438634.
  48. ↑ Bennett-Lovsey R, Hart SE, Shirai H, Mizuguchi K (April 2002). "The SWIB and the MDM2 domains are homologous and share a common fold". Bioinformatics. 18 (4): 626–630. doi: 10.1093/bioinformatics/18.4.626 . PMID   12016060.
  49. 1 2 Decristofaro MF, Betz BL, Rorie CJ, Reisman DN, Wang W, Weissman BE (January 2001). "Characterization of SWI/SNF protein expression in human breast cancer cell lines and other malignancies". Journal of Cellular Physiology. 186 (1): 136–145. doi:10.1002/1097-4652(200101)186:1<136::AID-JCP1010>3.0.CO;2-4. PMID   11147808. S2CID   25016283.
  50. ↑ Pagliaroli L, Porazzi P, Curtis AT, Scopa C, Mikkers HM, Freund C, et al. (November 2021). "Inability to switch from ARID1A-BAF to ARID1B-BAF impairs exit from pluripotency and commitment towards neural crest formation in ARID1B-related neurodevelopmental disorders". Nature Communications. 12 (1): 6469. Bibcode:2021NatCo..12.6469P. doi:10.1038/s41467-021-26810-x. PMC   8578637 . PMID   34753942.
  51. ↑ Woodley CM, Romer AS, Wang J, Guarnaccia AD, Elion DL, Maxwell JN, et al. (May 2021). "Multiple interactions of the oncoprotein transcription factor MYC with the SWI/SNF chromatin remodeler". Oncogene. 40 (20): 3593–3609. doi:10.1038/s41388-021-01804-7. PMC   8141032 . PMID   33931740.
  52. ↑ Vierbuchen T, Ling E, Cowley CJ, Couch CH, Wang X, Harmin DA, et al. (December 2017). "AP-1 Transcription Factors and the BAF Complex Mediate Signal-Dependent Enhancer Selection". Molecular Cell. 68 (6): 1067–1082.e12. doi:10.1016/j.molcel.2017.11.026. PMC   5744881 . PMID   29272704.
  53. ↑ "Table 1 The different components in the yeast, Drosophila and mammalian SWI/SNF complex". Oncogene Including Oncogene Reviews. ISSN   1476-5594.
  54. ↑ Collingwood TN, Urnov FD, Wolffe AP (December 1999). "Nuclear receptors: coactivators, corepressors and chromatin remodeling in the control of transcription". Journal of Molecular Endocrinology. 23 (3): 255–275. doi: 10.1677/jme.0.0230255 . PMID   10601972.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.