Actin, alpha 1

Actin, alpha skeletal muscle is a protein that in humans is encoded by the ACTA1 gene.[5][6]

ACTA1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesACTA1, ACTA, ASMA, CFTD, CFTD1, CFTDM, MPFD, NEM1, NEM2, NEM3, Actin, alpha 1, SHPM, actin, alpha 1, skeletal muscle, actin alpha 1, skeletal muscle
External IDsOMIM: 102610 MGI: 87902 HomoloGene: 121702 GeneCards: ACTA1
Gene location (Human)
Chr.Chromosome 1 (human)[1]
Band1q42.13Start229,431,245 bp[1]
End229,434,098 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

58

11459

Ensembl

ENSG00000143632

ENSMUSG00000031972

UniProt

P68133

P68134

RefSeq (mRNA)

NM_001100

NM_001272041
NM_009606

RefSeq (protein)

NP_001091

NP_001258970
NP_033736

Location (UCSC)Chr 1: 229.43 – 229.43 MbChr 8: 123.89 – 123.89 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Actin alpha 1 which is expressed in skeletal muscle is one of six different actin isoforms which have been identified. Actins are highly conserved proteins that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.[7]

Skeletal actin gene expression

Skeletal alpha actin expression is induced by stimuli and conditions known to cause muscle formation.[8] Such conditions result in fusion of committed cells (satellite cells) into myotubes, to form muscle fibers. Skeletal actin itself, when expressed, causes expression of several other "myogenic genes", which are essential to muscle formation.[9] One key transcription factor that activates skeletal actin gene expression is Serum Response Factor ("SRF"), a protein that binds to specific sites on the promoter DNA of the actin gene.[10] SRF may bring a number of other proteins to the promoter of skeletal actin, such as androgen receptor, and thereby contribute to induction of skeletal actin gene expression by androgenic (often termed "anabolic") steroids.[11]

Interactions

Actin, alpha 1 has been shown to interact with TMSB4X,[12][13] MIB2[14] and PRKCE.[15]

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gollark: Well, multiple devices.
gollark: The "distributed" means that multiple people are doing it, not that multiple people are affected.
gollark: If one idiot runs a thing which saturates the server's network connection, it is not in fact "distributed".

See also

References
  1. GRCh38: Ensembl release 89: ENSG00000143632 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000031972 - 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. Mogensen J, Kruse TA, Børglum AD (March 1999). "Assignment of the human skeletal muscle [FC12]a-actin gene (ACTA1) to chromosome 1q42.13-->q42.2 by radiation hybrid mapping". Cytogenetics and Cell Genetics. 83 (3–4): 224–5. doi:10.1159/000015184. PMID 10072583.
  6. Gunning P, Ponte P, Okayama H, Engel J, Blau H, Kedes L (May 1983). "Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed". Molecular and Cellular Biology. 3 (5): 787–95. doi:10.1128/mcb.3.5.787. PMC 368601. PMID 6865942.
  7. "Entrez Gene: ACTA1 actin, alpha 1, skeletal muscle".
  8. Bandman E (December 1992). "Contractile protein isoforms in muscle development". Developmental Biology. 154 (2): 273–83. doi:10.1016/0012-1606(92)90067-Q. PMID 1358730.
  9. Gunning PW, Ferguson V, Brennan KJ, Hardeman EC (February 2001). "Alpha-skeletal actin induces a subset of muscle genes independently of muscle differentiation and withdrawal from the cell cycle". Journal of Cell Science. 114 (Pt 3): 513–24. PMID 11171321.
  10. Belaguli NS, Zhou W, Trinh TH, Majesky MW, Schwartz RJ (July 1999). "Dominant negative murine serum response factor: alternative splicing within the activation domain inhibits transactivation of serum response factor binding targets". Molecular and Cellular Biology. 19 (7): 4582–91. doi:10.1128/mcb.19.7.4582. PMC 84256. PMID 10373507.
  11. Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ (March 2005). "Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene". The Journal of Biological Chemistry. 280 (9): 7786–92. doi:10.1074/jbc.M413992200. PMID 15623502.
  12. Ballweber E, Hannappel E, Huff T, Stephan H, Haener M, Taschner N, Stoffler D, Aebi U, Mannherz HG (January 2002). "Polymerisation of chemically cross-linked actin:thymosin beta(4) complex to filamentous actin: alteration in helical parameters and visualisation of thymosin beta(4) binding on F-actin". Journal of Molecular Biology. 315 (4): 613–25. doi:10.1006/jmbi.2001.5281. PMID 11812134.
  13. Safer D, Sosnick TR, Elzinga M (May 1997). "Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends". Biochemistry. 36 (19): 5806–16. doi:10.1021/bi970185v. PMID 9153421.
  14. Takeuchi T, Heng HH, Ye CJ, Liang SB, Iwata J, Sonobe H, Ohtsuki Y (October 2003). "Down-regulation of a novel actin-binding molecule, skeletrophin, in malignant melanoma". The American Journal of Pathology. 163 (4): 1395–404. doi:10.1016/S0002-9440(10)63497-9. PMC 1868282. PMID 14507647.
  15. England K, Ashford D, Kidd D, Rumsby M (June 2002). "PKC epsilon is associated with myosin IIA and actin in fibroblasts". Cellular Signalling. 14 (6): 529–36. doi:10.1016/S0898-6568(01)00277-7. PMID 11897493.

Further reading
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