Beta-actin

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Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

Beta-actin (human gene and protein symbol ACTB/ACTB) 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.

Interactions

Beta-actin has been shown to interact with SPTBN2. In addition, RNA-binding protein Sam68 was found to interact with the mRNA encoding β-actin, which regulates the synaptic formation of the dendritic spines with its cytoskeletal components.

Beta-actin has been shown to activate eNOS, thereby increasing NO production. An eight-amino acid residue (326-333) in actin has been shown to mediate the interaction between actin and eNOS

Clinical relevance

Recurrent mutations in this gene have been associated to cases of diffuse large B-cell lymphoma.

Applications

Beta actin is usually used as a loading control, for among others, the integrity of cells, protein degradation, in PCR and Western blotting. Its molecular weight is approximately 42 kDa.

External links

• Human ACTB genome location and ACTB gene details page in the UCSC Genome Browser.

Further reading

• Vandekerckhove J, Leavitt J, Kakunaga T, Weber K (1980). "Coexpression of a mutant beta-actin and the two normal beta- and gamma-cytoplasmic actins in a stably transformed human cell line". Cell. 22 (3): 893–9. doi:10.1016/0092-8674(80)90566-8. PMID 6893954.
• Leavitt J, Gunning P, Porreca P, Ng SY, Lin CS, Kedes L (1984). "Molecular cloning and characterization of mutant and wild-type human beta-actin genes". Mol Cell Biology. 4 (10): 1961–9. doi:10.1128/mcb.4.10.1961. PMC 369012. PMID 6095033.
• Ng SY, Gunning P, Eddy R, Ponte P, Leavitt J, Shows T, Kedes L (1985). "Evolution of the functional human beta-actin gene and its multi-pseudogene family: conservation of noncoding regions and chromosomal dispersion of pseudogenes". Mol Cell Biology. 5 (10): 2720–32. doi:10.1128/mcb.5.10.2720. PMC 367010. PMID 3837182.
• 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.
• Gunning P, Weinberger R, Jeffrey P (Apr 1997). "Actin and tropomyosin isoforms in morphogenesis". Anatomy and Embryology. 195 (4): 311–5. doi:10.1007/s004290050050. PMID 9108196.
• Kimura T, Hashimoto I, Nishikawa M, Fujisawa JI (1997). "A role for Rev in the association of HIV-1 gag mRNA with cytoskeletal beta-actin and viral protein expression". Biochimie. 78 (11–12): 1075–80. doi:10.1016/S0300-9084(97)86732-6. PMID 9150887.
• Szentirmay MN, Sawadogo M (May 2000). "Spatial organization of RNA polymerase II transcription in the nucleus". Nucleic Acids Research. 28 (10): 2019–25. doi:10.1093/nar/28.10.2019. PMC 105382. PMID 10773068.
• Anderson JL, Hope TJ (Apr 2004). "HIV accessory proteins and surviving the host cell". Current HIV/AIDS Reports. 1 (1): 47–53. doi:10.1007/s11904-004-0007-x. PMID 16091223.
• Pederson T, Aebi U (Nov 2005). "Nuclear actin extends, with no contraction in sight". Molecular Biology of the Cell. 16 (11): 5055–60. doi:10.1091/mbc.E05-07-0656. PMC 1266405. PMID 16148048.
• Perrin BJ, Ervasti JM (Oct 2010). "The actin gene family: function follows isoform". Cytoskeleton. 67 (10): 630–4. doi:10.1002/cm.20475. PMC 2949686. PMID 20737541.

See also

• Actin
• ACTA1