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Interaction of STOP with neuronal tubulin is independent of polyglutamylation.

Authors :
Bonnet C
Denarier E
Bosc C
Lazereg S
Denoulet P
Larcher JC
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2002 Oct 04; Vol. 297 (4), pp. 787-93.
Publication Year :
2002

Abstract

In eukaryotes, the coordinated progress of the various cellular tasks along with the assembly of adapted cytoskeletal networks requires a tight regulation of the interactions between microtubules and their associated proteins. Polyglutamylation is the major post-translational modification of neuronal tubulin. Due to its oligomeric structure, polyglutamylation can serve as a potentiometer to modulate binding of diverse MAPs. In addition, it can exert a differential mode of regulation towards distinct microtubule protein partners. To find out to what extent polyglutamylation is a general regulator, we have analyzed its ability to affect the binding of STOPs, the major factors that confer cold- and nocodazole-resistance to microtubules. We have shown by blot overlay experiments that binding of STOP does not depend on the length of the polyglutamyl chains carried by tubulins. And contrary to the other microtubule-associated proteins tested so far, STOP can bind quantitatively to any tubulin isoform whatever its degree of polyglutamylation.

Details

Language :
English
ISSN :
0006-291X
Volume :
297
Issue :
4
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
12359221
Full Text :
https://doi.org/10.1016/s0006-291x(02)02294-5