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J. Biol. Chem., Vol. 280, Issue 27, 25604-25610, July 8, 2005

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 280/27/25604    most recent M500232200v1 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 Soulet, F. Articles by Bouche, G. Search for Related Content PubMed PubMed Citation Articles by Soulet, F. Articles by Bouche, G. Social Bookmarking                      What's this?

Exogenously Added Fibroblast Growth Factor 2 (FGF-2) to NIH3T3 Cells Interacts with Nuclear Ribosomal S6 Kinase 2 (RSK2) in a Cell Cycle-dependent Manner^*

Fabienne Soulet, Karine Bailly, Stéphane Roga, Anne-Claire Lavigne, François Amalric, and Gérard Bouche

From the Laboratoire de Biologie Vasculaire, Institut de Pharmacologie et de Biologie Structurale, Unité Mixte de Recherche 5089, 205 Route de Narbonne, 31077 Toulouse, France

Fibroblast growth factor 2 (FGF-2) has been detected in the nuclei of many tissues and cell lines. Here we demonstrate that FGF-2 added exogenously to NIH3T3 cells enters the nucleus and interacts with the nuclear active 90-kDa ribosomal S6 kinase 2 (RSK2) in a cell cycle-dependent manner. By using purified proteins, FGF-2 is shown to directly interact through two separate domains with two RSK2 domains on both sides of the hydrophobic motif, namely the NH₂-terminal kinase domain (residues 360–381) by amino acid Ser-117 and the COOH-terminal kinase domain (residues 388–400) by amino acids Leu-127 and Lys-128. Moreover, this interaction leads to maintenance of the sustained activation of RSK2 in G₁ phase of the cell cycle. FGF-2 mutants (FGF-2 S117A, FGF-2 L127A, and FGF-2 K128A) that fail to interact in vitro with RSK2 fail to maintain a sustained RSK2 activity in vivo.

Received for publication, January 7, 2005 , and in revised form, May 4, 2005.

^* This work was supported by grants from CNRS, Université Paul Sabatier, Ligue contre le Cancer, Association pour la Recherche sur le Cancer, and Conseil Régional Midi Pyrénées. 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 www.jbc.org) contains supplemental Fig. S1 ("FGF-2 S1127A does not interact with RSTK-2 (1–389 NTK), and FGF-2 L127A and K128A destabilize the interaction with RSK-2 (–HM CTK)").

To whom correspondence should be addressed. Tel.: 33-5-6117-5950; Fax: 33-5-6117-5994; E-mail: Gerard.Bouche{at}ipbs.fr.

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