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Localization of β tubulin in the cochlea and cultured cells with a novel monoclonal antibody

Cell Motility and the Cytoskeleton, ISSN: 0886-1544, Vol: 65, Issue: 6, Page: 505-514
2008
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Article Description

Tubulin, the dimeric structural protein of microtubules, is a heterodimer of α and β subunits; both α and β exist as numerous isotypes encoded by different genes. In vertebrates the sequence differences among the β, β, β, β and βV isotypes are highly conserved in evolution, implying that the isotypes may have functional significance. Isotype-specific monoclonal antibodies have been useful in determining the cellular and sub-cellular distributions and possible functions of the β; β, β, and β isotypes; however, little is known about the β isotype. We here report the creation and purification of a monoclonal antibody (SHM.12G11) specific for β. The antibody was designed to be specific for the C-terminal sequence EEEINE, which is unique to rodent and chicken β. The antibody was found to bind specifically to the C-terminal peptide EEEINE, and does not cross-react with the carboxy-termini of either α-tubulin or the other β-tubulin isotypes. However, the antibody also binds to the peptide EEEVNE, but not to the peptide EEEIDG, corresponding respectively to the C-terminal peptides of bovine and human β. Immunofluorescence analysis indicates that β is found in microtubules of both the interphase network and the mitotic spindle. In gerbils, β also occurs in the cochlea where it is found largely in the specialized cells that are unique in containing bundled microtubules with 15 protofilaments. © 2008 Wiley-Liss, Inc.

Bibliographic Details

Banerjee, Asok; Jensen-Smith, Heather; Lazzell, Anna; Prasad, Veena; Elguezabal, Gerardo; Hallworth, Richard; Ludueña, Richard F

Wiley

Biochemistry, Genetics and Molecular Biology

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