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PMID: 8365473 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Phosphorylation of GDI and membrane cycling of rab proteins.

FEBS letters ·Vol. 329 ·No. 3 ·1993-08-30 ·Pages 313-8

Steele-Mortimer O, Gruenberg J, Clague MJ

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals Cell Membrane/metabolism Cells, Cultured Cricetinae GTP-Binding Proteins/metabolism Isoelectric Focusing Membrane Proteins/metabolism Molecular Sequence Data Phosphoproteins/metabolism Precipitin Tests rab5 GTP-Binding Proteins
Chemicals
Membrane Proteins Phosphoproteins GTP-Binding Proteins rab5 GTP-Binding Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Steele-Mortimer O
Cell Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany.
Gruenberg J
Clague M J
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1993-08-30
Pages
313-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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