HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: fj.06-7667comv1 21/11/2787    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Chambraud, B. Articles by Baulieu, E. E. Search for Related Content PubMed PubMed Citation Articles by Chambraud, B. Articles by Baulieu, E. E.

The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation

Béatrice Chambraud^*, Hamida Belabes^*, Virginie Fontaine-Lenoir, Arlette Fellous and Etienne Emile Baulieu^*,,1

^* INSERM, Unité mixte de recherche 788, Université ParisXI, Kremlin Bicêtre, France; and

MAPREG Company, Centre Hospitalier Universitaire de Bicêtre, Bâtiment Paul Langevin, Le Kremlin Bicêtre Cedex, France

¹Correspondence: INSERM, Unité mixte de recherche 788, Université ParisXI, 80 rue du Général leclerc, Kremlin Bicêtre 94276, France. E-mail: baulieu{at}kb.inserm.fr

The FK506 binding protein FKBP52 belongs to the large family of immunophilins and is known as a steroid receptor-associated protein. Previous data suggest that FKBP52 is associated with the motor protein dynein and with the cytoskeleton during mitosis. Here we demonstrate a specific and direct interaction between FKBP52 and tubulin. The region of FKBP52 located between aa 267 and 400, which includes the tetratricopeptide repeat domain, is required for tubulin binding. We provide evidence that FKBP52 prevents tubulin polymerization and that an 84 residue sequence located in the C-terminal part of the molecule (aa 375–458) is necessary and sufficient for its microtubule depolymerization activity. In colocalization experiments in PC12 cells, FKBP52 is associated with tubulin in motile cellular compartments. Furthermore, we suggest that, by using siRNA, a decrease of FKBP52 expression in PC12 cells may lead to differentiated cell phenotype characterized by neurite extensions. Collectively, our data define an unexpected property of FKBP52 as a novel regulator of microtubule dynamics. The possible role of microtubule formation and tubulin binding of other immunophilins such as FKBP12 and FKBP51 is discussed.—Chambraud, B., Belabes, H., Fontaine-Lenoir, V., Fellous, A., Baulieu, E. E. The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation.

Key Words: cytoskeleton • neurite differentiation • microtubule dynamics • FK506 binding protein

This article has been cited by other articles:

				D. L. Riggs, M. B. Cox, H. L. Tardif, M. Hessling, J. Buchner, and D. F. Smith Noncatalytic Role of the FKBP52 Peptidyl-Prolyl Isomerase Domain in the Regulation of Steroid Hormone Signaling Mol. Cell. Biol., December 15, 2007; 27(24): 8658 - 8669. [Abstract] [Full Text] [PDF]