The stress-induced MAP kinase p38 regulates endocytic trafficking via the GDI:Rab5 complex

Valeria Cavalli, Francis Vilbois, Michela Corti, Maria J. Marcote, Kumiko Tamura, Michael Karin, Steve Arkinstall, Jean Gruenberg

Research output: Contribution to journalArticlepeer-review

208 Scopus citations

Abstract

Early endocytic membrane traffic is regulated by the small GTPase Rab5, which cycles between GTP- and GDP-bound states as well as between membrane and cytosol. The latter cycle depends on GDI, which functions as a Rab vehicle in the aqueous environment of the cytosol. Here, we report that formation of the GDI:Rab5 complex is stimulated by a cytosolic factor that we purified and then identified as p38 MAPK. We find that p38 regulates GDI in the cytosolic cycle of Rab5 and modulates endocytosis in vivo. Our observations reveal the existence of a cross-talk between endocytosis and the p38-dependent stress response, thus providing molecular evidence that endocytosis can be regulated by the environment.

Original languageEnglish
Pages (from-to)421-432
Number of pages12
JournalMolecular cell
Volume7
Issue number2
DOIs
StatePublished - 2001

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