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

J. Biol. Chem., Vol. 279, Issue 41, 43168-43177, October 8, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/41/43168    most recent M401915200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Steindler, C. Articles by Pellegrini, S. Search for Related Content PubMed PubMed Citation Articles by Steindler, C. Articles by Pellegrini, S. Social Bookmarking                      What's this?

Jamip1 (Marlin-1) Defines a Family of Proteins Interacting with Janus Kinases and Microtubules^*

Corinna Steindler, Zhi Li¶, Michèle Algarté, Andrès Alcover||, Valentina Libri**, Josiane Ragimbeau, and Sandra Pellegrini

From the Unité de Signalisation des Cytokines, CNRS URA 1961 and the ^||Unité de Biologie des Interactions Cellulaires, CNRS URA 2582, Institut Pasteur, Paris 75724 Cedex 15, France

Jamip1 (Jak and microtubule interacting protein), an alias of Marlin-1, was identified for its ability to bind to the FERM (band 4.1 ezrin/radixin/moesin) homology domain of Tyk2, a member of the Janus kinase (Jak) family of non-receptor tyrosine kinases that are central elements of cytokine signaling cascades. Jamip1 belongs to a family of three genes conserved in vertebrates and is predominantly expressed in neural tissues and lymphoid organs. Jamip proteins lack known domains and are extremely rich in predicted coiled coils that mediate dimerization. In our initial characterization of Jamip1 (73 kDa), we found that it comprises an N-terminal region that targets the protein to microtubule polymers and, when overexpressed in fibroblasts, profoundly perturbs the microtubule network, inducing the formation of tight and stable bundles. Jamip1 was shown to associate with two Jak family members, Tyk2 and Jak1, in Jurkat T cells via its C-terminal region. The restricted expression of Jamip1 and its ability to associate to and modify microtubule polymers suggest a specialized function of these proteins in dynamic processes, e.g. cell polarization, segregation of signaling complexes, and vesicle traffic, some of which may involve Jak tyrosine kinases.

Received for publication, February 20, 2004 , and in revised form, July 6, 2004.

^* This work was supported by grants from the Association pour la Recherche sur le Cancer (to S. P.) and the Ligue Nationale contre le Cancer (to A. A.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by the Ligue Nationale contre le Cancer and Marie Curie Individual Training Grant HPMF-CT-2001-01112.

^¶ Supported by a Manlio-Cantarini fellowship.

^** Supported by Fondation pour la Recherche Médicale.

To whom correspondence should be addressed: Unité de Signalisation des Cytokines, Institut Pasteur, 25 Rue du Docteur Roux, Paris 75724 Cedex 15, France. Tel.: 33-1-40613305; Fax: 33-1-40613204; E-mail: pellegri{at}pasteur.fr.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				Y. Nishimura, C. L. Martin, A. Vazquez-Lopez, S. J. Spence, A. I. Alvarez-Retuerto, M. Sigman, C. Steindler, S. Pellegrini, N. C. Schanen, S. T. Warren, et al. Genome-wide expression profiling of lymphoblastoid cell lines distinguishes different forms of autism and reveals shared pathways Hum. Mol. Genet., July 15, 2007; 16(14): 1682 - 1698. [Abstract] [Full Text] [PDF]