PHOSPHORYLATION OF GDI AND MEMBRANE CYCLING OF RAB PROTEINS

被引：46

作者：

STEELEMORTIMER, O

GRUENBERG, J

CLAGUE, MJ

机构：

[1] Cell Biology Programme, European Molecular Biology Laboratory, Heidelberg, 69012

来源：

FEBS LETTERS | 1993年 / 329卷 / 03期

关键词：

SMALL GTP-BINDING PROTEIN; RAB5; RAB GDI; MEMBRANE TRAFFIC;

D O I：

10.1016/0014-5793(93)80244-O

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Membrane transport is known to be regulated by protein phosphorylation and by small GTPases of the rab family. Using specific antibodies, we have identified a 55 kDa phosphorylated protein which co-immunoprecipitated with the cytosolic forms of rab5 and other rab proteins. We demonstrate, on the basis of its mobility in two-dimensional electrophoresis gels and its immunological properties, that this protein is rab GDI (p55/GDI). We also found that, a minor fraction of p55/GDI is membrane associated, but, whilst also complexed with rab proteins, it is not phosphorylated. On the basis of these data we suggest that the cycling of rab proteins between membranes and cytosol is regulated by phosphorylation of p55/GDI.

引用

页码：313 / 318

页数：6

共 24 条

[1]

ARAKI S, 1990, J BIOL CHEM, V265, P13007

[2] MUTATIONAL ANALYSIS OF THE PUTATIVE EFFECTOR DOMAIN OF THE GTP-BINDING YPT1 PROTEIN IN YEAST SUGGESTS SPECIFIC REGULATION BY A NOVEL GAP ACTIVITY [J].