Cap-Gly proteins at microtubule plus ends: is EB1 detyrosination involved? - Archive ouverte HAL Access content directly
Journal Articles PLoS ONE Year : 2012

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

(1) , (1) , (1) , (1) , (2) , (1)
1
2

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.
Fichier principal
Vignette du fichier
Bosson_et_al_CAP-GLY_proteins_2012.ME.pdf (502.22 Ko) Télécharger le fichier
Origin : Publisher files allowed on an open archive
Loading...

Dates and versions

inserm-00734122 , version 1 (20-09-2012)

Identifiers

Cite

Anouk Bosson, Jean-Marc Soleilhac, Odile Valiron, Didier Job, Annie Andrieux, et al.. Cap-Gly proteins at microtubule plus ends: is EB1 detyrosination involved?. PLoS ONE, 2012, 7 (3), pp.e33490. ⟨10.1371/journal.pone.0033490⟩. ⟨inserm-00734122⟩
176 View
150 Download

Altmetric

Share

Gmail Facebook Twitter LinkedIn More