Beta-actin (gene name 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 proteins1 that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.2
Beta-actin has been shown to interact with SPTBN2.34 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 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 kD.
References
^Hanukoglu I, Tanese N, Fuchs E (February 1983). "Complementary DNA sequence of a human cytoplasmic actin. Interspecies divergence of 3' non-coding regions". J. Mol. Biol.163 (4): 673–8. PMID6842590.
^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". Nature411 (6835): 321–5. doi:10.1038/35077108. PMID11357136.
^Holleran EA, Ligon LA, Tokito M, Stankewich MC, Morrow JS, Holzbaur EL (September 2001). "beta III spectrin binds to the Arp1 subunit of dynactin". J. Biol. Chem.276 (39): 36598–605. doi:10.1074/jbc.M104838200. PMID11461920.
^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 (March 2012). "Discovery and prioritization of somatic mutations in diffuse large B-cell lymphoma (DLBCL) by whole-exome sequencing". Proc. Natl. Acad. Sci. U.S.A.109 (10): 3879–84. doi:10.1073/pnas.1121343109. PMC3309757. PMID22343534.
Further reading
Snásel J, Pichová I (1997). "The cleavage of host cell proteins by HIV-1 protease.". Folia Biol. (Praha)42 (5): 227–30. doi:10.1007/BF02818986. PMID8997639.
Gunning P, Weinberger R, Jeffrey P (1997). "Actin and tropomyosin isoforms in morphogenesis.". Anat. Embryol.195 (4): 311–5. doi:10.1007/s004290050050. PMID9108196.
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.". Biochimie78 (11–12): 1075–80. doi:10.1016/S0300-9084(97)86732-6. PMID9150887.
Anderson JL, Hope TJ (2005). "HIV accessory proteins and surviving the host cell". Current HIV/AIDS reports1 (1): 47–53. doi:10.1007/s11904-004-0007-x. PMID16091223.
1atn: Atomic structure of the actin:DNASE I complex
1c0f: CRYSTAL STRUCTURE OF DICTYOSTELIUM CAATP-ACTIN IN COMPLEX WITH GELSOLIN SEGMENT 1
1c0g: CRYSTAL STRUCTURE OF 1:1 COMPLEX BETWEEN GELSOLIN SEGMENT 1 AND A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 228: Q228K/T229A/A230Y/E360H)
1d4x: Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution.
1dej: CRYSTAL STRUCTURE OF A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 646: Q228K/T229A/A230Y/A231K/S232E/E360H) IN COMPLEX WITH HUMAN GELSOLIN SEGMENT 1
1eqy: COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLIN DOMAIN 1