Thymopoietin

Last updated
TMPO
Protein TMPO PDB 1gjj.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases TMPO , CMD1T, LAP2, LEMD4, PRO0868, TP, thymopoietin
External IDs OMIM: 188380 MGI: 106920 HomoloGene: 31144 GeneCards: TMPO
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001032283
NM_001032284
NM_001307975
NM_003276

RefSeq (protein)
Location (UCSC) Chr 12: 98.52 – 98.55 Mb Chr 10: 90.98 – 91.02 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Lamina-associated polypeptide 2 (LAP2), isoforms beta/gamma is a protein that in humans is encoded by the TMPO gene. [5] [6] LAP2 is an inner nuclear membrane (INM) protein. [7]

Contents

Thymopoietin is a protein involved in the induction of CD90 in the thymus. The thymopoetin (TMPO) gene encodes three alternatively spliced mRNAs encoding proteins of 75 kDa (alpha), 51 kDa (beta) and 39 kDa (gamma) which are ubiquitously expressed in all cells. The human TMPO gene maps to chromosome band 12q22 and consists of eight exons. TMPO alpha is present diffusely expressed with the cell nucleus while TMPO beta and gamma are localized to the nuclear membrane. TMPO beta is a human homolog of the murine protein LAP2. LAP2 plays a role in the regulation of nuclear architecture by binding lamin B1 and chromosomes. This interaction is regulated by phosphorylation during mitosis. Given the nuclear localization of the three TMPO isoforms, it is unlikely that these proteins play any role in CD90 induction.

Interactions

Thymopoietin has been shown to interact with Barrier to autointegration factor 1, [8] AKAP8L, [9] [10] LMNB1 [11] [12] and LMNA. [13] [14]

Related Research Articles

<span class="mw-page-title-main">Telophase</span> Final stage of a cell division for eukaryotic cells both in mitosis and meiosis

Telophase is the final stage in both meiosis and mitosis in a eukaryotic cell. During telophase, the effects of prophase and prometaphase are reversed. As chromosomes reach the cell poles, a nuclear envelope is re-assembled around each set of chromatids, the nucleoli reappear, and chromosomes begin to decondense back into the expanded chromatin that is present during interphase. The mitotic spindle is disassembled and remaining spindle microtubules are depolymerized. Telophase accounts for approximately 2% of the cell cycle's duration.

<span class="mw-page-title-main">Lamin</span>

Lamins, also known as nuclear lamins are fibrous proteins in type V intermediate filaments, providing structural function and transcriptional regulation in the cell nucleus. Nuclear lamins interact with inner nuclear membrane proteins to form the nuclear lamina on the interior of the nuclear envelope. Lamins have elastic and mechanosensitive properties, and can alter gene regulation in a feedback response to mechanical cues. Lamins are present in all animals but are not found in microorganisms, plants or fungi. Lamin proteins are involved in the disassembling and reforming of the nuclear envelope during mitosis, the positioning of nuclear pores, and programmed cell death. Mutations in lamin genes can result in several genetic laminopathies, which may be life-threatening.

<span class="mw-page-title-main">Intermediate filament</span> Cytoskeletal structure

Intermediate filaments (IFs) are cytoskeletal structural components found in the cells of vertebrates, and many invertebrates. Homologues of the IF protein have been noted in an invertebrate, the cephalochordate Branchiostoma.

<span class="mw-page-title-main">Nuclear lamina</span>

The nuclear lamina is a dense fibrillar network inside the nucleus of eukaryote cells. It is composed of intermediate filaments and membrane associated proteins. Besides providing mechanical support, the nuclear lamina regulates important cellular events such as DNA replication and cell division. Additionally, it participates in chromatin organization and it anchors the nuclear pore complexes embedded in the nuclear envelope.

In biology, the nuclear matrix is the network of fibres found throughout the inside of a cell nucleus after a specific method of chemical extraction. According to some it is somewhat analogous to the cell cytoskeleton. In contrast to the cytoskeleton, however, the nuclear matrix has been proposed to be a dynamic structure. Along with the nuclear lamina, it supposedly aids in organizing the genetic information within the cell.

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

Emerin is a protein that in humans is encoded by the EMD gene, also known as the STA gene. Emerin, together with LEMD3, is a LEM domain-containing integral protein of the inner nuclear membrane in vertebrates. Emerin is highly expressed in cardiac and skeletal muscle. In cardiac muscle, emerin localizes to adherens junctions within intercalated discs where it appears to function in mechanotransduction of cellular strain and in beta-catenin signaling. Mutations in emerin cause X-linked recessive Emery–Dreifuss muscular dystrophy, cardiac conduction abnormalities and dilated cardiomyopathy.

<span class="mw-page-title-main">Laminopathy</span> Medical condition

Laminopathies are a group of rare genetic disorders caused by mutations in genes encoding proteins of the nuclear lamina. They are included in the more generic term nuclear envelopathies that was coined in 2000 for diseases associated with defects of the nuclear envelope. Since the first reports of laminopathies in the late 1990s, increased research efforts have started to uncover the vital role of nuclear envelope proteins in cell and tissue integrity in animals.

<span class="mw-page-title-main">Prelamin-A/C</span> Filament protein

Prelamin-A/C, or lamin A/C is a protein that in humans is encoded by the LMNA gene. Lamin A/C belongs to the lamin family of proteins.

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

Lamin-B receptor is a protein, and in humans, it is encoded by the LBR gene.

<span class="mw-page-title-main">LEM domain-containing protein 3</span>

LEM domain-containing protein 3 (LEMD3), also known as MAN1, is an integral protein in the inner nuclear membrane (INM) of the nuclear envelope. It is encoded by the LEMD3 gene and was first identified after it was isolated from the serum of a patient with a collagen vascular disease.

<span class="mw-page-title-main">Barrier to autointegration factor 1</span> Protein-coding gene in the species Homo sapiens

Barrier-to-autointegration factor is a protein that in humans is encoded by the BANF1 gene. It is a member of the barrier-to-autointegration factor family of proteins.

<span class="mw-page-title-main">CHAF1A</span> Protein-coding gene in the species Homo sapiens

Chromatin assembly factor 1 subunit A is a protein that in humans is encoded by the CHAF1A gene.

<span class="mw-page-title-main">CHAF1B</span> Protein-coding gene in the species Homo sapiens

Chromatin assembly factor 1 subunit B is a protein that in humans is encoded by the CHAF1B gene.

<span class="mw-page-title-main">AKAP8L</span> Protein-coding gene in the species Homo sapiens

A-kinase anchor protein 8-like is a protein that in humans is encoded by the AKAP8L gene.

<span class="mw-page-title-main">CBX5 (gene)</span> Protein-coding gene in humans

Chromobox protein homolog 5 is a protein that in humans is encoded by the CBX5 gene. It is a highly conserved, non-histone protein part of the heterochromatin family. The protein itself is more commonly called HP1α. Heterochromatin protein-1 (HP1) has an N-terminal domain that acts on methylated lysines residues leading to epigenetic repression. The C-terminal of this protein has a chromo shadow-domain (CSD) that is responsible for homodimerizing, as well as interacting with a variety of chromatin-associated, non-histone proteins.

<span class="mw-page-title-main">TOR1AIP1</span> Protein-coding gene in the species Homo sapiens

Torsin-1A-interacting protein 1 is a protein that in humans is encoded by the TOR1AIP1 gene. More commonly known as lamina associated polypeptide 1 (LAP1), it is a type II integral membrane protein that resides in the inner nuclear membrane. The luminal domain of LAP1 interacts with Torsin A and is necessary for the ATPase activity of Torsin A. LAP1 plays a critical role in skeletal and heart muscle. Mutations in TOR1AIP1 have been linked to muscular dystrophy and cardiomyopathy. It's deletion from mouse hepatocytes leads to defected very-low density lipoprotein secretion and causes non-alcoholic fatty liver disease and non-alcoholic steatohepatitis

<span class="mw-page-title-main">Lamin B1</span> Protein-coding gene in the species Homo sapiens

Lamin-B1 is a protein that in humans is encoded by the LMNB1 gene.

<span class="mw-page-title-main">Inner nuclear membrane protein</span> Protein embedded in inner membrane of nuclear envelope

Inner nuclear membrane proteins are membrane proteins that are embedded in or associated with the inner membrane of the nuclear envelope. There are about 60 INM proteins, most of which are poorly characterized with respect to structure and function. Among the few well-characterized INM proteins are lamin B receptor (LBR), lamina-associated polypeptide 1 (LAP1), lamina-associated polypeptide-2 (LAP2), emerin and MAN1.

<span class="mw-page-title-main">Barrier-to-autointegration factor</span> Family of proteins

In molecular biology, barrier-to-autointegration factor (BAF) is a family of essential proteins that is highly conserved in metazoan evolution, and which may act as DNA-bridging proteins. BAF binds directly to double-stranded DNA, to transcription activators, and to inner nuclear membrane proteins, including lamin A filaments that anchor nuclear pore complexes in place, and nuclear LEM-domain proteins that bind to lamin filaments and chromatin. New findings suggest that BAF has structural roles in nuclear assembly and chromatin organization, represses gene expression and might interlink chromatin structure, nuclear architecture and gene regulation in metazoans.

<span class="mw-page-title-main">Nuclear organization</span> Spatial distribution of chromatin within a cell nucleus

Nuclear organization refers to the spatial distribution of chromatin within a cell nucleus. There are many different levels and scales of nuclear organisation. Chromatin is a higher order structure of DNA.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000120802 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000019961 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Harris CA, Andryuk PJ, Cline S, Chan HK, Natarajan A, Siekierka JJ, Goldstein G (Jul 1994). "Three distinct human thymopoietins are derived from alternatively spliced mRNAs". Proceedings of the National Academy of Sciences of the United States of America. 91 (14): 6283–7. Bibcode:1994PNAS...91.6283H. doi: 10.1073/pnas.91.14.6283 . PMC   44185 . PMID   7517549.
  6. "Entrez Gene: TMPO thymopoietin".
  7. Holmer L, Worman HJ (Nov 2001). "Inner nuclear membrane proteins: functions and targeting". Cellular and Molecular Life Sciences. 58 (12–13): 1741–7. doi:10.1007/PL00000813. PMID   11766875. S2CID   20902309.
  8. Furukawa K (Aug 1999). "LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction". Journal of Cell Science. 112 ( Pt 15) (15): 2485–92. doi:10.1242/jcs.112.15.2485. PMID   10393804.
  9. Martins SB, Eide T, Steen RL, Jahnsen T, Skålhegg BS, Collas P (Nov 2000). "HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics". Journal of Cell Science. 113 Pt 21 (21): 3703–13. doi: 10.1242/jcs.113.21.3703 . PMID   11034899.
  10. Martins S, Eikvar S, Furukawa K, Collas P (Jan 2003). "HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication". The Journal of Cell Biology. 160 (2): 177–88. doi:10.1083/jcb.200210026. PMC   2172640 . PMID   12538639.
  11. Furukawa K, Kondo T (Feb 1998). "Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin". European Journal of Biochemistry. 251 (3): 729–33. doi: 10.1046/j.1432-1327.1998.2510729.x . PMID   9490046.
  12. Foisner R, Gerace L (Jul 1993). "Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation". Cell. 73 (7): 1267–79. doi:10.1016/0092-8674(93)90355-T. PMID   8324822. S2CID   10641633.
  13. Markiewicz E, Dechat T, Foisner R, Quinlan RA, Hutchison CJ (Dec 2002). "Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein". Molecular Biology of the Cell. 13 (12): 4401–13. doi:10.1091/mbc.E02-07-0450. PMC   138642 . PMID   12475961.
  14. Dechat T, Korbei B, Vaughan OA, Vlcek S, Hutchison CJ, Foisner R (Oct 2000). "Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins". Journal of Cell Science. 113 Pt 19 (19): 3473–84. doi:10.1242/jcs.113.19.3473. PMID   10984438.

Further reading