Actin, alpha skeletal muscle

Last updated
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, actin alpha 1, skeletal muscle
External IDs OMIM: 102610 MGI: 87902 HomoloGene: 121702 GeneCards: ACTA1
Orthologs
SpeciesHumanMouse
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]

Contents

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]

See also

Related Research Articles

<span class="mw-page-title-main">Actin</span> Family of proteins

Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm.

<span class="mw-page-title-main">Nebulin</span> Protein-coding gene in the species Homo sapiens

Nebulin is an actin-binding protein which is localized to the thin filament of the sarcomeres in skeletal muscle. Nebulin in humans is coded for by the gene NEB. It is a very large protein and binds as many as 200 actin monomers. Because its length is proportional to thin filament length, it is believed that nebulin acts as a thin filament "ruler" and regulates thin filament length during sarcomere assembly and acts as the coats the actin filament. Other functions of nebulin, such as a role in cell signaling, remain uncertain.

<span class="mw-page-title-main">Myogenin</span> Mammalian protein found in Homo sapiens

Myogenin, is a transcriptional activator encoded by the MYOG gene. Myogenin is a muscle-specific basic-helix-loop-helix (bHLH) transcription factor involved in the coordination of skeletal muscle development or myogenesis and repair. Myogenin is a member of the MyoD family of transcription factors, which also includes MyoD, Myf5, and MRF4.

<span class="mw-page-title-main">CEBPB</span> Protein-coding gene in the species Homo sapiens

CCAAT/enhancer-binding protein beta is a protein that in humans is encoded by the CEBPB gene.

<span class="mw-page-title-main">Beta-actin</span> Protein-coding gene in the species Homo sapiens

Actin beta is one of six different actin isoforms which have been identified in humans. This is one of the two nonmuscle cytoskeletal actins. Actins are highly conserved proteins that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.

<span class="mw-page-title-main">Serum response factor</span> Mammalian protein found in Homo sapiens

Serum response factor, also known as SRF, is a transcription factor protein.

<span class="mw-page-title-main">Actin, cytoplasmic 2</span> Protein-coding gene in the species Homo sapiens

Actin, cytoplasmic 2, or gamma-actin is a protein that in humans is encoded by the ACTG1 gene. Gamma-actin is widely expressed in cellular cytoskeletons of many tissues; in adult striated muscle cells, gamma-actin is localized to Z-discs and costamere structures, which are responsible for force transduction and transmission in muscle cells. Mutations in ACTG1 have been associated with nonsyndromic hearing loss and Baraitser-Winter syndrome, as well as susceptibility of adolescent patients to vincristine toxicity.

<span class="mw-page-title-main">Alpha-actinin-1</span> Protein-coding gene in the species Homo sapiens

Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.

<span class="mw-page-title-main">Eukaryotic translation elongation factor 1 alpha 1</span> Constitutive promoter

Elongation factor 1-alpha 1 (eEF1a1) is a translation elongation protein, expressed across eukaryotes. In humans, it is encoded by the EEF1A1 gene.

<span class="mw-page-title-main">ACTC1</span> Protein-coding gene in the species Homo sapiens

ACTC1 encodes cardiac muscle alpha actin. This isoform differs from the alpha actin that is expressed in skeletal muscle, ACTA1. Alpha cardiac actin is the major protein of the thin filament in cardiac sarcomeres, which are responsible for muscle contraction and generation of force to support the pump function of the heart.

<span class="mw-page-title-main">Tropomyosin 3</span> Protein-coding gene in the species Homo sapiens

Tropomyosin alpha-3 chain is a protein that in humans is encoded by the TPM3 gene.

<span class="mw-page-title-main">ACTA2</span> Protein-coding gene in the species Homo sapiens

ACTA2 is an actin protein with several aliases including alpha-actin, alpha-actin-2,aortic smooth muscle or alpha smooth muscle actin. Actins are a family of globular multi-functional proteins that form microfilaments. ACTA2 is one of 6 different actin isoforms and is involved in the contractile apparatus of smooth muscle. ACTA2 is extremely highly conserved and found in nearly all mammals.

<span class="mw-page-title-main">FLNC (gene)</span> Protein-coding gene in the species Homo sapiens

Filamin-C (FLN-C) also known as actin-binding-like protein (ABPL) or filamin-2 (FLN2) is a protein that in humans is encoded by the FLNC gene. Filamin-C is mainly expressed in cardiac and skeletal muscles, and functions at Z-discs and in subsarcolemmal regions.

<span class="mw-page-title-main">TPM2</span> Protein-coding gene in the species Homo sapiens

β-Tropomyosin, also known as tropomyosin beta chain is a protein that in humans is encoded by the TPM2 gene. β-tropomyosin is striated muscle-specific coiled coil dimer that functions to stabilize actin filaments and regulate muscle contraction.

<span class="mw-page-title-main">TEAD1</span> Protein-coding gene in the species Homo sapiens

Transcriptional enhancer factor TEF-1 also known as TEA domain family member 1 (TEAD1) and transcription factor 13 (TCF-13) is a protein that in humans is encoded by the TEAD1 gene. TEAD1 was the first member of the TEAD family of transcription factors to be identified.

<span class="mw-page-title-main">CAPZA2</span> Protein-coding gene in the species Homo sapiens

F-actin-capping protein subunit alpha-2 also known as CapZ-alpha2 is a protein that in humans is encoded by the CAPZA2 gene.

<span class="mw-page-title-main">Troponin C, skeletal muscle</span> Protein-coding gene in the species Homo sapiens

Troponin C, skeletal muscle is a protein that in humans is encoded by the TNNC2 gene.

<span class="mw-page-title-main">TLN1</span> Protein-coding gene in the species Homo sapiens

Talin-1 is a protein that in humans is encoded by the TLN1 gene. Talin-1 is ubiquitously expressed, and is localized to costamere structures in cardiac and skeletal muscle cells, and to focal adhesions in smooth muscle and non-muscle cells. Talin-1 functions to mediate cell-cell adhesion via the linkage of integrins to the actin cytoskeleton and in the activation of integrins. Altered expression of talin-1 has been observed in patients with heart failure, however no mutations in TLN1 have been linked with specific diseases.

<span class="mw-page-title-main">Thymosin beta-4</span> Mammalian protein found in Homo sapiens

Thymosin beta-4 is a protein that in humans is encoded by the TMSB4X gene. Recommended INN for thymosin beta-4 is 'timbetasin', as published by the World Health Organization (WHO).

<span class="mw-page-title-main">TLN2</span> Protein-coding gene in the species Homo sapiens

Talin-2 is a protein in humans that is encoded by the TLN2 gene. It belongs to the talin protein family. This gene encodes a protein related to talin-1, a cytoskeletal protein that plays a significant role in the assembly of actin filaments. Talin-2 is expressed at high levels in cardiac muscle and functions to provide linkages between the extracellular matrix and actin cytoskeleton at costamere structures to transduce force laterally.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000143632 - Ensembl, May 2017
  2. 1 2 3 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.

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