Actin, alpha skeletal muscle is a protein that in humans is encoded by the ACTA1gene.
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.
Skeletal alpha actin expression is induced by stimuli and conditions known to cause muscle formation. 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. 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. SRF may bring a number of other proteins to the promoter of skeletal actin, such as andogen receptor, and thereby contribute to induction of skeletal actin gene expression by androgenic (often termed "anabolic") steroids.
^Mogensen J, Kruse TA, Borglum (March 1999). "Assignment of the human skeletal muscle [FC12]a-actin gene (ACTA1) to chromosome 1q42.13-->q42.2 by radiation hybrid mapping". Cytogenet Cell Genet83 (3-4): 224–5. doi:10.1159/000015184. PMID10072583.
^Gunning, PW; Ferguson, V; Brennan, KJ; Hardeman, EC (2001). "Alpha-skeletal actin induces a subset of muscle genes independently of muscle differentiation and withdrawal from the cell cycle.". Journal of Cell Science114 (Pt 3): 513–24. PMID11171321.
^Vlahopoulos, S; Zimmer, WE; Jenster, G; Belaguli, NS; Balk, SP; Brinkmann, AO; Lanz, RB; Zoumpourlis, VC; Schwartz, RJ (2005). "Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene.". The Journal of Biological Chemistry280 (9): 7786–92. doi:10.1074/jbc.M413992200. PMID15623502.
^Ballweber, Edda; Hannappel Ewald, Huff Thomas, Stephan Harald, Haener Markus, Taschner Nicole, Stoffler Daniel, Aebi Ueli, Mannherz Hans Georg (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". J. Mol. Biol. (England) 315 (4): 613–25. doi:10.1006/jmbi.2001.5281. ISSN0022-2836. PMID11812134.Cite uses deprecated parameters (help)
^Safer, D; Sosnick T R; Elzinga M (May 1997). "Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends". Biochemistry (UNITED STATES) 36 (19): 5806–16. doi:10.1021/bi970185v. ISSN0006-2960. PMID9153421.
Adams LD, Tomasselli AG, Robbins P, et al. (1992). "HIV-1 protease cleaves actin during acute infection of human T-lymphocytes.". AIDS Res. Hum. Retroviruses8 (2): 291–5. doi:10.1089/aid.1992.8.291. PMID1540415.
Levine BA, Moir AJ, Patchell VB, Perry SV (1992). "Binding sites involved in the interaction of actin with the N-terminal region of dystrophin.". FEBS Lett.298 (1): 44–8. doi:10.1016/0014-5793(92)80019-D. PMID1544421.
Rijken PJ, Hage WJ, van Bergen en Henegouwen PM, et al. (1992). "Epidermal growth factor induces rapid reorganization of the actin microfilament system in human A431 cells.". J. Cell. Sci.100 (3): 491–9. PMID1808202.
Tomasselli AG, Hui JO, Adams L, et al. (1991). "Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus.". J. Biol. Chem.266 (22): 14548–53. PMID1907279.
Taylor A, Erba HP, Muscat GE, Kedes L (1989). "Nucleotide sequence and expression of the human skeletal alpha-actin gene: evolution of functional regulatory domains.". Genomics3 (4): 323–36. doi:10.1016/0888-7543(88)90123-1. PMID2907503.
Bretscher A, Weber K (1980). "Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner.". Cell20 (3): 839–47. doi:10.1016/0092-8674(80)90330-X. PMID6893424.