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

@article{Cavalli2001TheSM,
  title={The stress-induced MAP kinase p38 regulates endocytic trafficking via the GDI:Rab5 complex.},
  author={Valeria Cavalli and Francis Vilbois and Michela Angela Maria Corti and Mar{\'i}a Jes{\'u}s Marcote and Kumiko Tamura and Michael Karin and Steve Arkinstall and Jean Gruenberg},
  journal={Molecular cell},
  year={2001},
  volume={7 2},
  pages={421-32}
}
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… CONTINUE READING
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