Beta-actin

ACTB
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesACTB, BRWS1, PS1TP5BP1, Beta-actin, actin, beta, actin beta
External IDsMGI: 87904 HomoloGene: 110648 GeneCards: ACTB
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
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 MbChr 5: 142.9 – 142.91 Mb
PubMed search[1][2]
Wikidata
View/Edit HumanView/Edit Mouse

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[3][4] that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.[5]

Interactions

Beta-actin has been shown to interact with SPTBN2.[6][7] 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[8]

Clinical relevance

Recurrent mutations in this gene have been associated to cases of diffuse large B-cell lymphoma.[9]

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. "Human PubMed Reference:".
  2. "Mouse PubMed Reference:".
  3. 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. PMID 25788699. doi:10.1242/jcs.165563.
  4. 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. PMID 6842590. doi:10.1016/0022-2836(83)90117-1.
  5. "Entrez Gene: ACTB actin, beta".
  6. 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. PMID 11357136. doi:10.1038/35077108.
  7. 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. PMID 11461920. doi:10.1074/jbc.M104838200.
  8. 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. PMC 2836036Freely accessible. PMID 19946124. doi:10.1074/jbc.M109.063172.
  9. 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. PMC 3309757Freely accessible. PMID 22343534. doi:10.1073/pnas.1121343109.

Further reading

See also


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