Actin, alpha skeletal muscle

ACTA1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1T44
Identifiers
Aliases	ACTA1 , ACTA, ASMA, CFTD, CFTD1, CFTDM, MPFD, NEM1, NEM2, NEM3, Actin, alpha 1, SHPM, actin, alpha 1, skeletal muscle, actin alpha 1, skeletal muscle
External IDs	OMIM: 102610; MGI: 87902; HomoloGene: 121702; GeneCards: ACTA1; OMA:ACTA1 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1q42.13 Start 229,430,365 bp [1] End 229,434,104 bp [1]
Gene location (Mouse) Chr. Chromosome 8 (mouse) [2] Band 8 E2|8 72.26 cM Start 124,618,508 bp [2] End 124,621,490 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Skeletal muscle tissue of biceps brachii glutes triceps brachii muscle Skeletal muscle tissue of rectus abdominis thoracic diaphragm tibialis anterior muscle muscle of thigh gastrocnemius muscle body of tongue deltoid muscle Top expressed in ankle soleus muscle plantaris muscle medial head of gastrocnemius muscle intercostal muscle muscle of thigh body of femur digastric muscle temporal muscle vastus lateralis muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding myosin binding ADP binding structural constituent of cytoskeleton protein binding ATP binding Cellular component cytoplasm cell body cytosol blood microparticle filopodium sarcomere striated muscle thin filament stress fiber extracellular fluid actin filament actin cytoskeleton extracellular exosome cytoskeleton lamellipodium Biological process muscle contraction response to steroid hormone skeletal muscle fiber adaptation response to mechanical stimulus skeletal muscle thin filament assembly response to lithium ion cell growth positive regulation of gene expression muscle filament sliding mesenchyme migration response to extracellular stimulus skeletal muscle fiber development Sources:Amigo / QuickGO
Orthologs Species Human Mouse 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 Mb Chr 8: 124.62 – 124.62 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

Clinical significance

Mutations in the ACTA1 gene are known to cause the following conditions: ^[16]

• Nemaline myopathy 3 (NEM3);
• Myopathy, actin, congenital, with excess of thin myofilaments (MPCETM);
• Myopathy, congenital, with fiber-type disproportion (CFTD);
• Myopathy, scapulohumeroperoneal (SHPM).

See also

• Actin
• ACTB

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. S2CID   84202330.
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. doi:10.1242/jcs.114.3.513. 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.
16. "UniProt". www.uniprot.org. Retrieved 2023-09-09.

Further reading

• Snásel J, Pichová I (1997). "The cleavage of host cell proteins by HIV-1 protease". Folia Biologica. 42 (5): 227–30. doi:10.1007/BF02818986. PMID   8997639. S2CID   7617882.
• 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. PMID   12127568.
• 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 . PMID   648524.
• den Hartigh JC, van Bergen en Henegouwen PM, Verkleij AJ, Boonstra J (October 1992). "The EGF receptor is an actin-binding protein". The Journal of Cell Biology. 119 (2): 349–55. doi:10.1083/jcb.119.2.349. PMC   2289650 . PMID   1383230.
• Adams LD, Tomasselli AG, Robbins P, Moss B, Heinrikson RL (February 1992). "HIV-1 protease cleaves actin during acute infection of human T-lymphocytes". AIDS Research and Human Retroviruses. 8 (2): 291–5. doi:10.1089/aid.1992.8.291. PMID   1540415.
• Levine BA, Moir AJ, Patchell VB, Perry SV (February 1992). "Binding sites involved in the interaction of actin with the N-terminal region of dystrophin". FEBS Letters. 298 (1): 44–8. doi: 10.1016/0014-5793(92)80019-D . PMID   1544421.
• Rijken PJ, Hage WJ, van Bergen en Henegouwen PM, Verkleij AJ, Boonstra J (November 1991). "Epidermal growth factor induces rapid reorganization of the actin microfilament system in human A431 cells". Journal of Cell Science. 100 ( Pt 3) (3): 491–9. doi: 10.1242/jcs.100.3.491 . PMID   1808202.
• Tomasselli AG, Hui JO, Adams L, Chosay J, Lowery D, Greenberg B, Yem A, Deibel MR, Zürcher-Neely H, Heinrikson RL (August 1991). "Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus". The Journal of Biological Chemistry. 266 (22): 14548–53. doi: 10.1016/S0021-9258(18)98721-1 . PMID   1907279.
• Shoeman RL, Kesselmier C, Mothes E, Höner B, Traub P (January 1991). "Non-viral cellular substrates for human immunodeficiency virus type 1 protease". FEBS Letters. 278 (2): 199–203. doi: 10.1016/0014-5793(91)80116-K . PMID   1991513.
• Winder SJ, Walsh MP (June 1990). "Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation". The Journal of Biological Chemistry. 265 (17): 10148–55. doi: 10.1016/S0021-9258(19)38792-7 . PMID   2161834.
• Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC (September 1990). "Atomic structure of the actin:DNase I complex". Nature. 347 (6288): 37–44. Bibcode:1990Natur.347...37K. doi:10.1038/347037a0. PMID   2395459. S2CID   925337.
• Takahashi K, Hiwada K, Kokubu T (June 1988). "Vascular smooth muscle calponin. A novel troponin T-like protein". Hypertension. 11 (6 Pt 2): 620–6. doi: 10.1161/01.hyp.11.6.620 . PMID   2455687.
• 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 . PMID   2907503.
• Shen BW, Josephs R, Steck TL (March 1986). "Ultrastructure of the intact skeleton of the human erythrocyte membrane". The Journal of Cell Biology. 102 (3): 997–1006. doi:10.1083/jcb.102.3.997. PMC   2114132 . PMID   2936753.
• Burgess DR, Broschat KO, Hayden JM (January 1987). "Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins". The Journal of Cell Biology. 104 (1): 29–40. doi:10.1083/jcb.104.1.29. PMC   2117036 . PMID   3793760.
• 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. PMID   3842206.
• Hanauer A, Levin M, Heilig R, Daegelen D, Kahn A, Mandel JL (June 1983). "Isolation and characterization of cDNA clones for human skeletal muscle alpha actin". Nucleic Acids Research. 11 (11): 3503–16. doi:10.1093/nar/11.11.3503. PMC   325982 . PMID   6190133.
• 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. PMID   6893424. S2CID   568395.

External links

• GeneReviews/NCBI/NIH/UW entry on Nemaline Myopathy
• Human ACTA1 genome location and ACTA1 gene details page in the UCSC Genome Browser .