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

Anouk Bosson 1 Jean-Marc Soleilhac 1 Odile Valiron 1 Didier Job 1 Annie Andrieux 2 Marie-Jo Moutin 1, *
* Corresponding author
1 INSERM U836, équipe 1, Physiopathologie du cytosquelette
GIN - Grenoble Institut des Neurosciences
2 INSERM U836, équipe 1, Physiopathologie du cytosquelette
GPC - Groupe Physiopathologie du Cytosquelette, GIN - Grenoble Institut des Neurosciences
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.
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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, Public Library of Science, 2012, 7 (3), pp.e33490. ⟨10.1371/journal.pone.0033490⟩. ⟨inserm-00734122⟩

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