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

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.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Cavalli V,Vilbois F,Corti M,Marcote MJ,Tamura K,Karin M,Arkinstall S,Gruenberg J

doi

10.1016/s1097-2765(01)00189-7

subject

Has Abstract

pub_date

2001-02-01 00:00:00

pages

421-32

issue

2

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(01)00189-7

journal_volume

7

pub_type

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