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Originally published In Press as doi:10.1074/jbc.M011380200 on January 22, 2001

J. Biol. Chem., Vol. 276, Issue 16, 12839-12848, April 20, 2001
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Differential Binding Regulation of Microtubule-associated Proteins MAP1A, MAP1B, and MAP2 by Tubulin Polyglutamylation*

Crystel BonnetDagger , Dominique BoucherDagger , Sylvie LazeregDagger , Barbara Pedrotti§, Khalid Islam, Philippe DenouletDagger , and Jean Christophe LarcherDagger ||

From the Dagger  Biochimie Cellulaire, CNRS FRE 2219, Université Pierre et Marie Curie, 9 quai Saint-Bernard, Case 265, 75252 Paris, Cedex 05, France, the § Department of Biology, University of Milano, 20133 Milano, Italy, and  Arpida AG, Dammstrasse 36, Munchenstein 4142, BL, Switzerland

The major neuronal post-translational modification of tubulin, polyglutamylation, can act as a molecular potentiometer to modulate microtubule-associated proteins (MAPs) binding as a function of the polyglutamyl chain length. The relative affinity of Tau, MAP2, and kinesin has been shown to be optimal for tubulin modified by ~3 glutamyl units. Using blot overlay assays, we have tested the ability of polyglutamylation to modulate the interaction of two other structural MAPs, MAP1A and MAP1B, with tubulin. MAP1A and MAP2 display distinct behavior in terms of tubulin binding; they do not compete with each other, even when the polyglutamyl chains of tubulin are removed, indicating that they have distinct binding sites on tubulin. Binding of MAP1A and MAP1B to tubulin is also controlled by polyglutamylation and, although the modulation of MAP1B binding resembles that of MAP2, we found that polyglutamylation can exert a different mode of regulation toward MAP1A. Interestingly, although the affinity of the other MAPs tested so far decreases sharply for tubulins carrying long polyglutamyl chains, the affinity of MAP1A for these tubulins is maintained at a significant level. This differential regulation exerted by polyglutamylation toward different MAPs might facilitate their selective recruitment into distinct microtubule populations, hence modulating their functional properties.

* This work was supported by CNRS FRE 2219 and by the Association pour la Recherche sur le Cancer (Grant ARC 9241).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Tel.: 33-1-44-27-22-94; Fax: 33-1-44-27-22-15; E-mail: jclarche@snv.jussieu.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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