Actin, alpha 1

From Wikipedia, the free encyclopedia
  (Redirected from ACTA1)
Jump to: navigation, search
ACTA1
PBB Protein ACTA1 image.jpg
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases ACTA1, ACTA, ASMA, CFTD, CFTD1, CFTDM, MPFD, NEM1, NEM2, NEM3, Actin, alpha 1, SHPM, actin, alpha 1, skeletal muscle
External IDs MGI: 87902 HomoloGene: 121702 GeneCards: ACTA1
RNA expression pattern
PBB GE ACTA1 203872 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001100

NM_001272041
NM_009606

RefSeq (protein)

NP_001091

NP_001258970.1
NP_033736.1
NP_001258970
NP_033736

Location (UCSC) Chr 1: 229.43 – 229.43 Mb Chr 8: 123.89 – 123.89 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Actin, alpha skeletal muscle is a protein that in humans is encoded by the ACTA1 gene.[3][4]

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.[5]

Skeletal actin gene expression[edit]

Skeletal alpha actin expression is induced by stimuli and conditions known to cause muscle formation.[6] 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.[7] 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.[8] 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.[9]

Interactions[edit]

Actin, alpha 1 has been shown to interact with TMSB4X,[10][11] MIB2[12] and PRKCE.[13]

See also[edit]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Mogensen J, Kruse TA, Borglum AD (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 Genet. 83 (3-4): 224–5. doi:10.1159/000015184. PMID 10072583. 
  4. ^ Gunning P, Ponte P, Okayama H, Engel J, Blau H, Kedes L (August 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". Mol Cell Biol. 3 (5): 787–95. doi:10.1128/mcb.3.5.787. PMC 368601Freely accessible. PMID 6865942. 
  5. ^ "Entrez Gene: ACTA1 actin, alpha 1, skeletal muscle". 
  6. ^ Bandman, E (1992). "Contractile protein isoforms in muscle development.". Developmental Biology. 154 (2): 273–83. doi:10.1016/0012-1606(92)90067-Q. PMID 1358730. 
  7. ^ 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 Science. 114 (Pt 3): 513–24. PMID 11171321. 
  8. ^ Belaguli, NS; Zhou, W; Trinh, TH; Majesky, MW; Schwartz, RJ (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. PMC 84256Freely accessible. PMID 10373507. 
  9. ^ 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 Chemistry. 280 (9): 7786–92. doi:10.1074/jbc.M413992200. PMID 15623502. 
  10. ^ 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. ISSN 0022-2836. PMID 11812134. 
  11. ^ 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. ISSN 0006-2960. PMID 9153421. 
  12. ^ Takeuchi, Tamotsu; Heng Henry H Q; Ye Christine J; Liang Sheng-Ben; Iwata Jun; Sonobe Hiroshi; Ohtsuki Yuji (October 2003). "Down-regulation of a novel actin-binding molecule, skeletrophin, in malignant melanoma". Am. J. Pathol. United States. 163 (4): 1395–404. doi:10.1016/S0002-9440(10)63497-9. ISSN 0002-9440. PMC 1868282Freely accessible. PMID 14507647. 
  13. ^ England, Karen; Ashford David; Kidd Daniel; Rumsby Martin (June 2002). "PKC epsilon is associated with myosin IIA and actin in fibroblasts". Cell. Signal. England. 14 (6): 529–36. doi:10.1016/S0898-6568(01)00277-7. ISSN 0898-6568. PMID 11897493. 

External links[edit]

Further reading[edit]