Beta-actin

Actin, beta
PDB rendering based on 1atn.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3BYH​, 3D2U​, 3J82​, 3LUE​
Identifiers
Symbols	ACTB ; BRWS1; PS1TP5BP1
External IDs	OMIM: 102630 MGI: 87904 HomoloGene: 110648 GeneCards: ACTB Gene
Gene ontology Molecular function • RNA polymerase II core promoter proximal region sequence-specific DNA binding • RNA polymerase II distal enhancer sequence-specific DNA binding • structural constituent of cytoskeleton • protein binding • ATP binding • kinesin binding • Tat protein binding • nucleosomal DNA binding • identical protein binding • nitric-oxide synthase binding Cellular component • nuclear chromatin • extracellular space • nucleoplasm • cytoplasm • cytosol • cytoskeleton • plasma membrane • focal adhesion • membrane • ribonucleoprotein complex • cortical cytoskeleton • NuA4 histone acetyltransferase complex • cytoplasmic ribonucleoprotein granule • myelin sheath • protein complex • extracellular exosome • MLL5-L complex • blood microparticle • dense body Biological process • retina homeostasis • chromatin organization • protein folding • movement of cell or subcellular component • small GTPase mediated signal transduction • axon guidance • blood coagulation • substantia nigra development • cell junction assembly • adherens junction organization • Fc-gamma receptor signaling pathway involved in phagocytosis • ATP-dependent chromatin remodeling • cellular protein metabolic process • innate immune response • cell-cell junction organization • vascular endothelial growth factor receptor signaling pathway • ephrin receptor signaling pathway • 'de novo' posttranslational protein folding • membrane organization • platelet aggregation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	60	11461
Ensembl	ENSG00000075624	ENSMUSG00000029580
UniProt	P60709	P60710
RefSeq (mRNA)	NM_001101	NM_007393
RefSeq (protein)	NP_001092	NP_031419
Location (UCSC)	Chr 7: 5.53 – 5.56 Mb	Chr 5: 142.9 – 142.91 Mb
PubMed search

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^[1][2] that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.^[3]

Interactions

Beta-actin has been shown to interact with SPTBN2.^[4][5] 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^[6]

Clinical relevance

Recurrent mutations in this gene have been associated to cases of diffuse large B-cell lymphoma.^[7]

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.

References

1. Gunning PW, Ghoshdastider U, Whitaker S, Popp D, Robinson RC (Jun 2015). "The evolution of compositionally and functionally distinct actin filaments". Journal of Cell Science 128 (11): 2009–2019. doi:10.1242/jcs.165563. PMID 25788699.
2. Hanukoglu I, Tanese N, Fuchs E (Feb 1983). "Complementary DNA sequence of a human cytoplasmic actin. Interspecies divergence of 3' non-coding regions". Journal of Molecular Biology 163 (4): 673–8. doi:10.1016/0022-2836(83)90117-1. PMID 6842590.
3. "Entrez Gene: ACTB actin, beta".
4. Mao B, Wu W, Li Y, Hoppe D, Stannek P, Glinka A, Niehrs C (May 2001). "LDL-receptor-related protein 6 is a receptor for Dickkopf proteins". Nature 411 (6835): 321–5. doi:10.1038/35077108. PMID 11357136.
5. Holleran EA, Ligon LA, Tokito M, Stankewich MC, Morrow JS, Holzbaur EL (Sep 2001). "beta III spectrin binds to the Arp1 subunit of dynactin". The Journal of Biological Chemistry 276 (39): 36598–605. doi:10.1074/jbc.M104838200. PMID 11461920.
6. Kondrikov D, Fonseca FV, Elms S, Fulton D, Black SM, Block ER, Su Y (Feb 2010). "Beta-actin association with endothelial nitric-oxide synthase modulates nitric oxide and superoxide generation from the enzyme". The Journal of Biological Chemistry 285 (7): 4319–27. doi:10.1074/jbc.M109.063172. PMID 19946124.
7. Lohr JG, Stojanov P, Lawrence MS, Auclair D, Chapuy B, Sougnez C, Cruz-Gordillo P, Knoechel B, Asmann YW, Slager SL, Novak AJ, Dogan A, Ansell SM, Link BK, Zou L, Gould J, Saksena G, Stransky N, Rangel-Escareño C, Fernandez-Lopez JC, Hidalgo-Miranda A, Melendez-Zajgla J, Hernández-Lemus E, Schwarz-Cruz y Celis A, Imaz-Rosshandler I, Ojesina AI, Jung J, Pedamallu CS, Lander ES, Habermann TM, Cerhan JR, Shipp MA, Getz G, Golub TR (Mar 2012). "Discovery and prioritization of somatic mutations in diffuse large B-cell lymphoma (DLBCL) by whole-exome sequencing". Proceedings of the National Academy of Sciences of the United States of America 109 (10): 3879–84. doi:10.1073/pnas.1121343109. PMC 3309757. PMID 22343534.

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. 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. 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