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Mol Biol Cell. 1994 Dec; 5(12): 1301–1310.
PMCID: PMC301159

Beta-centractin: characterization and distribution of a new member of the centractin family of actin-related proteins.


An examination of human-expressed sequence tags indicated the existence of an isoform of centractin, an actin-related protein localized to microtubule-associated structures. Using one of these tags, we isolated and determined the nucleotide sequence of a full-length cDNA clone. The protein encoded represents the first example of multiple isoforms of an actin-related protein in a single organism. Northern analysis using centractin-specific probes revealed three species of mRNA in HeLa cells that could encode centractin isoforms. One mRNA encodes the previously-identified centractin (now referred to as alpha-centractin). The full-length cDNA clone isolated using the expressed sequence tag encodes a new member of the centractin family, beta-centractin. A probe specific for alpha-centractin hybridized to the third species of mRNA observed (referred to as gamma-centractin). Comparisons of Northern blots of human tissues indicated that alpha-centractin and beta-centractin mRNAs are equally distributed in all populations of mRNA examined, whereas the expression of gamma-centractin appears to be tissue specific. The amino acid sequence of beta-centractin, deduced from the cDNA, indicates a 91% identity with alpha-centractin, increasing to 96% similarity when conservative amino acid changes are taken into account. As antibodies previously raised against alpha-centractin reacted only poorly with beta-centractin, new antibodies were produced and combined with two-dimensional gel electrophoresis to discriminate the two isoforms. Using this system, the subcellular distribution of the alpha- and beta-isoforms were determined. Both isoforms were found predominantly in the cytosolic fraction as a part of a previously identified 20S complex (referred to as the dynactin complex) with no evidence for a free pool of either isoform. The isoforms were found in a constant ratio of approximately 15:1 (alpha:beta) in the dynactin complex.

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  • Adams MD, Dubnick M, Kerlavage AR, Moreno R, Kelley JM, Utterback TR, Nagle JW, Fields C, Venter JC. Sequence identification of 2,375 human brain genes. Nature. 1992 Feb 13;355(6361):632–634. [PubMed]
  • Ansorge W. Fast and sensitive detection of protein and DNA bands by treatment with potassium permanganate. J Biochem Biophys Methods. 1985 May;11(1):13–20. [PubMed]
  • Bornens M, Paintrand M, Berges J, Marty MC, Karsenti E. Structural and chemical characterization of isolated centrosomes. Cell Motil Cytoskeleton. 1987;8(3):238–249. [PubMed]
  • Buchanan BB, Eiermann W, Riccio P, Aquila H, Klingenberg M. Antibody evidence for different conformational states of ADP, ATP translocator protein isolated from mitochondria. Proc Natl Acad Sci U S A. 1976 Jul;73(7):2280–2284. [PMC free article] [PubMed]
  • Buckingham ME. Actin and myosin multigene families: their expression during the formation of skeletal muscle. Essays Biochem. 1985;20:77–109. [PubMed]
  • Clark SW, Meyer DI. Centractin is an actin homologue associated with the centrosome. Nature. 1992 Sep 17;359(6392):246–250. [PubMed]
  • Clark SW, Meyer DI. Long lost cousins of actin. Curr Biol. 1993 Jan;3(1):54–55. [PubMed]
  • Collins CA, Vallee RB. Preparation of microtubules from rat liver and testis: cytoplasmic dynein is a major microtubule associated protein. Cell Motil Cytoskeleton. 1989;14(4):491–500. [PubMed]
  • Frangioni JV, Neel BG. Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal Biochem. 1993 Apr;210(1):179–187. [PubMed]
  • Gill SR, Schroer TA, Szilak I, Steuer ER, Sheetz MP, Cleveland DW. Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J Cell Biol. 1991 Dec;115(6):1639–1650. [PMC free article] [PubMed]
  • Guan KL, Dixon JE. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal Biochem. 1991 Feb 1;192(2):262–267. [PubMed]
  • Herman IM. Actin isoforms. Curr Opin Cell Biol. 1993 Feb;5(1):48–55. [PubMed]
  • Hortsch M, Avossa D, Meyer DI. Characterization of secretory protein translocation: ribosome-membrane interaction in endoplasmic reticulum. J Cell Biol. 1986 Jul;103(1):241–253. [PMC free article] [PubMed]
  • Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC. Atomic structure of the actin:DNase I complex. Nature. 1990 Sep 6;347(6288):37–44. [PubMed]
  • Lees-Miller JP, Helfman DM, Schroer TA. A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility. Nature. 1992 Sep 17;359(6392):244–246. [PubMed]
  • O'Farrell PH. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed]
  • Paschal BM, Holzbaur EL, Pfister KK, Clark S, Meyer DI, Vallee RB. Characterization of a 50-kDa polypeptide in cytoplasmic dynein preparations reveals a complex with p150GLUED and a novel actin. J Biol Chem. 1993 Jul 15;268(20):15318–15323. [PubMed]
  • Paschal BM, Shpetner HS, Vallee RB. Purification of brain cytoplasmic dynein and characterization of its in vitro properties. Methods Enzymol. 1991;196:181–191. [PubMed]
  • Schafer DA, Gill SR, Cooper JA, Heuser JE, Schroer TA. Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin. J Cell Biol. 1994 Jul;126(2):403–412. [PMC free article] [PubMed]
  • Studier FW, Moffatt BA. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol. 1986 May 5;189(1):113–130. [PubMed]
  • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. [PMC free article] [PubMed]
  • Wickens M. How the messenger got its tail: addition of poly(A) in the nucleus. Trends Biochem Sci. 1990 Jul;15(7):277–281. [PubMed]

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