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Actin, alpha skeletal muscle
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<h2 id="skeletal-actin-gene-expression">Skeletal actin gene expression</h2> <p>Skeletal alpha actin expression is induced by stimuli and conditions known to cause muscle formation.<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> 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.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> 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.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> 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.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> </p> <h2 id="interactions">Interactions</h2> <p>Actin, alpha 1 has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with <a href="/facts/TMSB4X/7grpwyq3">TMSB4X</a>,<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a><a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> <a href="/facts/MIB2_(gene)/QEcFgBzt">MIB2</a><a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> and <a href="/facts/PRKCE/sSH90sKv">PRKCE</a>.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> </p> <h2 id="clinical-significance">Clinical significance</h2> <p>Mutations in the ACTA1 gene are known to cause the following conditions:<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> </p> <ul><li>Nemaline myopathy 3 (NEM3);</li> <li>Myopathy, actin, congenital, with excess of thin myofilaments (MPCETM);</li> <li>Myopathy, congenital, with fiber-type disproportion (CFTD);</li> <li>Myopathy, scapulohumeroperoneal (SHPM).</li></ul> <h2 id="see-also">See also</h2> <ul><li><a href="/facts/Actin/Hu3qIUL9">Actin</a></li> <li><a href="/facts/ACTB/xl4lpRHC">ACTB</a></li></ul> <h2 id="further-reading">Further reading</h2> <ul><li>Snásel J, Pichová I (1997). "The cleavage of host cell proteins by HIV-1 protease". <i>Folia Biologica</i>. 42 (5): 227–30. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1007%2FBF02818986">10.1007/BF02818986</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8997639">8997639</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:7617882">7617882</a>.</li> <li>Di Fiore PP, Scita G (October 2002). "Eps8 in the midst of GTPases". <i>The International Journal of Biochemistry & Cell Biology</i>. 34 (10): 1178–83. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS1357-2725%2802%2900064-X">10.1016/S1357-2725(02)00064-X</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12127568">12127568</a>.</li> <li>Ogawa H, Shiraki H, Matsuda Y, Nakagawa H (April 1978). <a href="https://doi.org/10.1111%2Fj.1432-1033.1978.tb12243.x">"Interaction of adenylosuccinate synthetase with F-actin"</a>. <i>European Journal of Biochemistry</i>. 85 (2): 331–7. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1111%2Fj.1432-1033.1978.tb12243.x">10.1111/j.1432-1033.1978.tb12243.x</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/648524">648524</a>.</li> <li>den Hartigh JC, van Bergen en Henegouwen PM, Verkleij AJ, Boonstra J (October 1992). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289650">"The EGF receptor is an actin-binding protein"</a>. <i>The Journal of Cell Biology</i>. 119 (2): 349–55. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1083%2Fjcb.119.2.349">10.1083/jcb.119.2.349</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289650">2289650</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1383230">1383230</a>.</li> <li>Adams LD, Tomasselli AG, Robbins P, Moss B, Heinrikson RL (February 1992). <a href="https://zenodo.org/record/1235231">"HIV-1 protease cleaves actin during acute infection of human T-lymphocytes"</a>. <i>AIDS Research and Human Retroviruses</i>. 8 (2): 291–5. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1089%2Faid.1992.8.291">10.1089/aid.1992.8.291</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1540415">1540415</a>.</li> <li>Levine BA, Moir AJ, Patchell VB, Perry SV (February 1992). <a href="https://doi.org/10.1016%2F0014-5793%2892%2980019-D">"Binding sites involved in the interaction of actin with the N-terminal region of dystrophin"</a>. <i>FEBS Letters</i>. 298 (1): 44–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0014-5793%2892%2980019-D">10.1016/0014-5793(92)80019-D</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1544421">1544421</a>.</li> <li>Rijken PJ, Hage WJ, van Bergen en Henegouwen PM, Verkleij AJ, Boonstra J (November 1991). <a href="https://doi.org/10.1242%2Fjcs.100.3.491">"Epidermal growth factor induces rapid reorganization of the actin microfilament system in human A431 cells"</a>. <i>Journal of Cell Science</i>. 100 ( Pt 3) (3): 491–9. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1242%2Fjcs.100.3.491">10.1242/jcs.100.3.491</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1808202">1808202</a>.</li> <li>Tomasselli AG, Hui JO, Adams L, Chosay J, Lowery D, Greenberg B, Yem A, Deibel MR, Zürcher-Neely H, Heinrikson RL (August 1991). <a href="https://doi.org/10.1016%2FS0021-9258%2818%2998721-1">"Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus"</a>. <i>The Journal of Biological Chemistry</i>. 266 (22): 14548–53. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0021-9258%2818%2998721-1">10.1016/S0021-9258(18)98721-1</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1907279">1907279</a>.</li> <li>Shoeman RL, Kesselmier C, Mothes E, Höner B, Traub P (January 1991). <a href="https://doi.org/10.1016%2F0014-5793%2891%2980116-K">"Non-viral cellular substrates for human immunodeficiency virus type 1 protease"</a>. <i>FEBS Letters</i>. 278 (2): 199–203. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0014-5793%2891%2980116-K">10.1016/0014-5793(91)80116-K</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1991513">1991513</a>.</li> <li>Winder SJ, Walsh MP (June 1990). <a href="https://doi.org/10.1016%2FS0021-9258%2819%2938792-7">"Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation"</a>. <i>The Journal of Biological Chemistry</i>. 265 (17): 10148–55. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0021-9258%2819%2938792-7">10.1016/S0021-9258(19)38792-7</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/2161834">2161834</a>.</li> <li>Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC (September 1990). "Atomic structure of the actin:DNase I complex". <i>Nature</i>. 347 (6288): 37–44. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1990Natur.347...37K">1990Natur.347...37K</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F347037a0">10.1038/347037a0</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/2395459">2395459</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:925337">925337</a>.</li> <li>Takahashi K, Hiwada K, Kokubu T (June 1988). <a href="https://doi.org/10.1161%2F01.hyp.11.6.620">"Vascular smooth muscle calponin. A novel troponin T-like protein"</a>. <i>Hypertension</i>. 11 (6 Pt 2): 620–6. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1161%2F01.hyp.11.6.620">10.1161/01.hyp.11.6.620</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/2455687">2455687</a>.</li> <li>Taylor A, Erba HP, Muscat GE, Kedes L (November 1988). <a href="https://doi.org/10.1016%2F0888-7543%2888%2990123-1">"Nucleotide sequence and expression of the human skeletal alpha-actin gene: evolution of functional regulatory domains"</a>. <i>Genomics</i>. 3 (4): 323–36. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0888-7543%2888%2990123-1">10.1016/0888-7543(88)90123-1</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/2907503">2907503</a>.</li> <li>Shen BW, Josephs R, Steck TL (March 1986). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114132">"Ultrastructure of the intact skeleton of the human erythrocyte membrane"</a>. <i>The Journal of Cell Biology</i>. 102 (3): 997–1006. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1083%2Fjcb.102.3.997">10.1083/jcb.102.3.997</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114132">2114132</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/2936753">2936753</a>.</li> <li>Burgess DR, Broschat KO, Hayden JM (January 1987). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2117036">"Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins"</a>. <i>The Journal of Cell Biology</i>. 104 (1): 29–40. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1083%2Fjcb.104.1.29">10.1083/jcb.104.1.29</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2117036">2117036</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/3793760">3793760</a>.</li> <li>Kedes L, Ng SY, Lin CS, Gunning P, Eddy R, Shows T, Leavitt J (1986). "The human beta-actin multigene family". <i>Transactions of the Association of American Physicians</i>. 98: 42–6. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/3842206">3842206</a>.</li> <li>Hanauer A, Levin M, Heilig R, Daegelen D, Kahn A, Mandel JL (June 1983). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC325982">"Isolation and characterization of cDNA clones for human skeletal muscle alpha actin"</a>. <i>Nucleic Acids Research</i>. 11 (11): 3503–16. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Fnar%2F11.11.3503">10.1093/nar/11.11.3503</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC325982">325982</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/6190133">6190133</a>.</li> <li>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". <i>Cell</i>. 20 (3): 839–47. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0092-8674%2880%2990330-X">10.1016/0092-8674(80)90330-X</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/6893424">6893424</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:568395">568395</a>.</li></ul> <h2 id="external-links">External links</h2> <ul><li><a href="https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=nem">GeneReviews/NCBI/NIH/UW entry on Nemaline Myopathy</a></li> <li>Human <a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&singleSearch=knownCanonical&position=ACTA1"><i>ACTA1</i></a> genome location and <a href="https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_type=knownGene&hgg_gene=ACTA1"><i>ACTA1</i></a> gene details page in the <a href="/facts/UCSC_Genome_Browser/kwumPyLb">UCSC Genome Browser</a>.</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>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. S2CID 84202330. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>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. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC368601" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC368601</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>"Entrez Gene: ACTA1 actin, alpha 1, skeletal muscle". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=58" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=58</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>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. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>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. doi:10.1242/jcs.114.3.513. PMID 11171321. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>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. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84256" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84256</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>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. <a href="https://doi.org/10.1074%2Fjbc.M413992200" target="_blank">https://doi.org/10.1074%2Fjbc.M413992200</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>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. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>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. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>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. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1868282" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1868282</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>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. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li> <li id="fn:12"><p>"UniProt". www.uniprot.org. Retrieved 2023-09-09. <a href="https://www.uniprot.org/uniprot/P68133" target="_blank">https://www.uniprot.org/uniprot/P68133</a> <a href="#fnref:12" class="footnote-back-ref">↩</a></p></li> </ol>