 |
Journal articles
Cap-Gly proteins at microtubule plus ends: is EB1 detyrosination involved?
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.
Cited literature [18 references]
https://www.hal.inserm.fr/inserm-00734122
Contributor : Annie Andrieux <>
Submitted on : Thursday, September 20, 2012 - 5:15:32 PM
Last modification on : Wednesday, December 2, 2020 - 4:34:02 PM
Long-term archiving on: : Friday, December 21, 2012 - 3:51:22 AM
Contributor : Annie Andrieux <>
Submitted on : Thursday, September 20, 2012 - 5:15:32 PM
Last modification on : Wednesday, December 2, 2020 - 4:34:02 PM
Long-term archiving on: : Friday, December 21, 2012 - 3:51:22 AM
File
Bosson_et_al_CAP-GLY_proteins_...
Publisher files allowed on an open archive