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

J. Biol. Chem., Vol. 283, Issue 46, 32131-32142, November 14, 2008

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 283/46/32131    most recent M802927200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted 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 Request Permissions Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Courchet, J. Articles by Billaud, M. Search for Related Content PubMed PubMed Citation Articles by Courchet, J. Articles by Billaud, M. Social Bookmarking                      What's this?

Interaction with 14-3-3 Adaptors Regulates the Sorting of hMex-3B RNA-binding Protein to Distinct Classes of RNA Granules^*

Julien Courchet¹, Karine Buchet-Poyau², Auriane Potemski, Aurélie Brès, Isabelle Jariel-Encontre, and Marc Billaud³

From the CNRS UMR5201, Laboratoire de Génétique Moléculaire, Signalisation et Cancer, Lyon F-69008, France, Universitéde Lyon, Lyon F-69008, France, Université Lyon 1, Domaine Rockefeller, Lyon F-69008, France, and Centre Léon Bérard, Lyon F-69008, France and Institut de Génétique Moléculaire de Montpellier, CNRS, 1919 Route de Mende, Montpellier F-34293, France

Stress granules (SG) and processing bodies (PBs) are cytoplasmic ribonucleoprotein particles whose assembly is induced by different stimuli. SG are the site of storage of untranslated transcripts formed in response to environmental stress, whereas PBs are involved in mRNA turnover. We recently characterized a novel family of four human proteins related to the Caenorhabditis elegans Mex-3, a RNA binding protein involved in the establishment of the anterior-posterior embryonic asymmetry and in the maintenance of germline pluripotency. We now report that the adaptor proteins 14-3-3 bind to hMex-3B but not to the three other hMex-3 family members. Serine 462, when phosphorylated, is the major 14-3-3 docking site on hMex-3B, and manipulation of this interaction reveals that 14-3-3 both stabilizes hMex-3B and modulates its ability to bind RNA. Furthermore, the complex formed between hMex-3B and Argonaute proteins is excluded from PBs when the interaction with 14-3-3 is disrupted, whereas the recruitment to SG is not affected. Thus, 14-3-3 exerts combined effects on hMex-3B and acts as a major regulator of the sorting between distinct classes of RNA granules.

Received for publication, April 16, 2008 , and in revised form, September 8, 2008.

^* 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental "Materials and Methods," Figs. 1-3, and Table 1.

¹ Recipient of a grant from the CNRS and from the Association pour la Recherche sur le Cancer.

² Recipient of a grant from the Centre Regional de Lutte contre le Cancer Léon Berard.

³ To whom correspondence should be addressed. E-mail: billaud{at}univ-lyon1.fr.

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