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PLoS One. 2012;7(3):e33490. doi: 10.1371/journal.pone.0033490. Epub 2012 Mar 14.

Cap-Gly proteins at microtubule plus ends: is EB1 detyrosination involved?

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1
Institut National de la Santé et de la Recherche Médicale (INSERM) U836, Université Joseph Fourier, Grenoble, France.

Abstract

Localization of CAP-Gly proteins such as CLIP170 at microtubule+ends results from their dual interaction with α-tubulin and EB1 through their C-terminal amino acids -EEY. Detyrosination (cleavage of the terminal tyrosine) of α-tubulin by tubulin-carboxypeptidase abolishes CLIP170 binding. Can detyrosination affect EB1 and thus regulate the presence of CLIP170 at microtubule+ends as well? We developed specific antibodies to discriminate tyrosinated vs detyrosinated forms of EB1 and detected only tyrosinated EB1 in fibroblasts, astrocytes, and total brain tissue. Over-expressed EB1 was not detyrosinated in cells and chimeric EB1 with the eight C-terminal amino acids of α-tubulin was only barely detyrosinated. Our results indicate that detyrosination regulates CLIPs interaction with α-tubulin, but not with EB1. They highlight the specificity of carboxypeptidase toward tubulin.

PMID:
22432029
PMCID:
PMC3303835
DOI:
10.1371/journal.pone.0033490
[Indexed for MEDLINE]
Free PMC Article
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