Actin, alpha skeletal muscle is a protein that in humans is encoded by the ACTA1gene.[5][6]
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 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]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^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. PMID10072583. S2CID84202330.
^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. PMID11812134.
^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. PMID9153421.
Di Fiore PP, Scita G (October 2002). "Eps8 in the midst of GTPases". The International Journal of Biochemistry & Cell Biology. 34 (10): 1178–83. doi:10.1016/S1357-2725(02)00064-X. PMID12127568.
Ogawa H, Shiraki H, Matsuda Y, Nakagawa H (April 1978). "Interaction of adenylosuccinate synthetase with F-actin". European Journal of Biochemistry. 85 (2): 331–7. doi:10.1111/j.1432-1033.1978.tb12243.x. PMID648524.
Taylor A, Erba HP, Muscat GE, Kedes L (November 1988). "Nucleotide sequence and expression of the human skeletal alpha-actin gene: evolution of functional regulatory domains". Genomics. 3 (4): 323–36. doi:10.1016/0888-7543(88)90123-1. PMID2907503.
Kedes L, Ng SY, Lin CS, Gunning P, Eddy R, Shows T, Leavitt J (1986). "The human beta-actin multigene family". Transactions of the Association of American Physicians. 98: 42–6. PMID3842206.
Bretscher A, Weber K (July 1980). "Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner". Cell. 20 (3): 839–47. doi:10.1016/0092-8674(80)90330-X. PMID6893424. S2CID568395.
PDB gallery
1atn: Atomic structure of the actin:DNASE I complex
1c0g: CRYSTAL STRUCTURE OF 1:1 COMPLEX BETWEEN GELSOLIN SEGMENT 1 AND A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 228: Q228K/T229A/A230Y/E360H)
1d4x: Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution.
1eqy: COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLIN DOMAIN 1