ACTA1

Actin, alpha 1, skeletal muscle, also known as ACTA1, is a human gene.

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: ACTA1 actin, alpha 1, skeletal muscle| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=58| accessdate = ]

Skeletal actin gene expression

Skeletal alpha actin expression is induced by stimuli and conditions known to cause muscle formation [Bandman E. Contractile protein isoforms in muscle development. Dev Biol. 1992 Dec;154(2):273-83. Review.PMID: 1358730 ] . 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 [Gunning PW, Ferguson V, Brennan KJ, Hardeman EC. Alpha-skeletal actin induces a subset of muscle genes independently of muscle differentiation and withdrawal from the cell cycle. J Cell Sci. 2001 Feb;114(Pt 3):513-24. PMID: 11171321 ] . 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 [Belaguli NS, Zhou W, Trinh TH, Majesky MW, Schwartz RJ. Dominant negative murine serum response factor: alternative splicing within the activation domain inhibits transactivation of serum response factor binding targets. Mol Cell Biol. 1999 Jul;19(7):4582-91. PMID: 10373507 ] . 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 [Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ. Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene. J Biol Chem. 2005 Mar 4;280(9):7786-92. Epub 2004 Dec 28. PMID: 15623502] .

ee also

*Actin
*ACTB

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Snásel J, Pichová I |title=The cleavage of host cell proteins by HIV-1 protease. |journal=Folia Biol. (Praha) |volume=42 |issue= 5 |pages= 227–30 |year= 1997 |pmid= 8997639 |doi=
*cite journal | author=Di Fiore PP, Scita G |title=Eps8 in the midst of GTPases. |journal=Int. J. Biochem. Cell Biol. |volume=34 |issue= 10 |pages= 1178–83 |year= 2002 |pmid= 12127568 |doi=
*cite journal | author=Ogawa H, Shiraki H, Matsuda Y, Nakagawa H |title=Interaction of adenylosuccinate synthetase with F-actin. |journal=Eur. J. Biochem. |volume=85 |issue= 2 |pages= 331–7 |year= 1978 |pmid= 648524 |doi=
*cite journal | author=Caccamise DA |title=My franchise was a teen-age lion's den. |journal=Dental economics - oral hygiene |volume=66 |issue= 11 |pages= 36–43 |year= 1978 |pmid= 1074709 |doi=
*cite journal | author=den Hartigh JC, van Bergen en Henegouwen PM, Verkleij AJ, Boonstra J |title=The EGF receptor is an actin-binding protein. |journal=J. Cell Biol. |volume=119 |issue= 2 |pages= 349–55 |year= 1992 |pmid= 1383230 |doi=
*cite journal | author=Adams LD, Tomasselli AG, Robbins P, "et al." |title=HIV-1 protease cleaves actin during acute infection of human T-lymphocytes. |journal=AIDS Res. Hum. Retroviruses |volume=8 |issue= 2 |pages= 291–5 |year= 1992 |pmid= 1540415 |doi=
*cite journal | author=Levine BA, Moir AJ, Patchell VB, Perry SV |title=Binding sites involved in the interaction of actin with the N-terminal region of dystrophin. |journal=FEBS Lett. |volume=298 |issue= 1 |pages= 44–8 |year= 1992 |pmid= 1544421 |doi=
*cite journal | author=Rijken PJ, Hage WJ, van Bergen en Henegouwen PM, "et al." |title=Epidermal growth factor induces rapid reorganization of the actin microfilament system in human A431 cells. |journal=J. Cell. Sci. |volume=100 ( Pt 3) |issue= |pages= 491–9 |year= 1992 |pmid= 1808202 |doi=
*cite journal | author=Tomasselli AG, Hui JO, Adams L, "et al." |title=Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14548–53 |year= 1991 |pmid= 1907279 |doi=
*cite journal | author=Shoeman RL, Kesselmier C, Mothes E, "et al." |title=Non-viral cellular substrates for human immunodeficiency virus type 1 protease. |journal=FEBS Lett. |volume=278 |issue= 2 |pages= 199–203 |year= 1991 |pmid= 1991513 |doi=
*cite journal | author=Winder SJ, Walsh MP |title=Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation. |journal=J. Biol. Chem. |volume=265 |issue= 17 |pages= 10148–55 |year= 1990 |pmid= 2161834 |doi=
*cite journal | author=Kabsch W, Mannherz HG, Suck D, "et al." |title=Atomic structure of the actin:DNase I complex. |journal=Nature |volume=347 |issue= 6288 |pages= 37–44 |year= 1990 |pmid= 2395459 |doi= 10.1038/347037a0
*cite journal | author=Takahashi K, Hiwada K, Kokubu T |title=Vascular smooth muscle calponin. A novel troponin T-like protein. |journal=Hypertension |volume=11 |issue= 6 Pt 2 |pages= 620–6 |year= 1988 |pmid= 2455687 |doi=
*cite journal | author=Taylor A, Erba HP, Muscat GE, Kedes L |title=Nucleotide sequence and expression of the human skeletal alpha-actin gene: evolution of functional regulatory domains. |journal=Genomics |volume=3 |issue= 4 |pages= 323–36 |year= 1989 |pmid= 2907503 |doi=
*cite journal | author=Shen BW, Josephs R, Steck TL |title=Ultrastructure of the intact skeleton of the human erythrocyte membrane. |journal=J. Cell Biol. |volume=102 |issue= 3 |pages= 997–1006 |year= 1986 |pmid= 2936753 |doi=
*cite journal | author=Burgess DR, Broschat KO, Hayden JM |title=Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins. |journal=J. Cell Biol. |volume=104 |issue= 1 |pages= 29–40 |year= 1987 |pmid= 3793760 |doi=
*cite journal | author=Kedes L, Ng SY, Lin CS, "et al." |title=The human beta-actin multigene family. |journal=Trans. Assoc. Am. Physicians |volume=98 |issue= |pages= 42–6 |year= 1986 |pmid= 3842206 |doi=
*cite journal | author=Hanauer A, Levin M, Heilig R, "et al." |title=Isolation and characterization of cDNA clones for human skeletal muscle alpha actin. |journal=Nucleic Acids Res. |volume=11 |issue= 11 |pages= 3503–16 |year= 1983 |pmid= 6190133 |doi=
*cite journal | author=Gunning P, Ponte P, Okayama H, "et al." |title=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. |journal=Mol. Cell. Biol. |volume=3 |issue= 5 |pages= 787–95 |year= 1983 |pmid= 6865942 |doi=
*cite journal | author=Bretscher A, Weber K |title=Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner. |journal=Cell |volume=20 |issue= 3 |pages= 839–47 |year= 1980 |pmid= 6893424 |doi=

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