Rab GDP dissociation inhibitor as a general regulator for the membrane association of rab proteins

Ullrich, Oliver, Stenmark, Harald, Alexandrov, Kirill, Huber, Lukas A, Kaibuchi, Kozo, Sasaki, Takuya, Takai, Yoshimi and Zerial, Marino (1993) Rab GDP dissociation inhibitor as a general regulator for the membrane association of rab proteins. Journal of Biological Chemistry, 268 24: 18143-18150.

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ336317_OA.pdf Full text (open access) application/pdf 5.37MB 0
Author Ullrich, Oliver
Stenmark, Harald
Alexandrov, Kirill
Huber, Lukas A
Kaibuchi, Kozo
Sasaki, Takuya
Takai, Yoshimi
Zerial, Marino
Title Rab GDP dissociation inhibitor as a general regulator for the membrane association of rab proteins
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 1993-08-25
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 268
Issue 24
Start page 18143
End page 18150
Total pages 8
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
Rab proteins comprise a family of small GTPases that serve a regulatory role in membrane traffic. These proteins are in part cytosolic and in part associated with the membranes of specific exocytic and endocytic organelles. Smg p25A/rab3A GDI, a cytosolic protein which inhibits the dissociation of GDP from smg p25A/rab3A, Sec4p, and rab11, has also been found to prevent association of rab3A with the membrane. In this study, we have used Madin- Darby canine kidney cells permeabilized with the bacterial toxin streptolysin O to test the general activity of rab3A GDI in modulating the membrane association of various small GTP-binding proteins. Rab3A GDP dissociation inhibitor (GDI) removed from the membrane all rab proteins we have tested and inhibited the membrane binding of in vitro translated rab proteins. However, rab3A GDI had a limited effect on the membrane association of a mutant rab5 protein which contained a farnesylated cysteine motif. Finally, we found that, although rab3A GDI resides primarily in the cytosol, it is also associated with compartments of the exocytic and endocytic pathways. Since rab3A GDI can modulate the membrane association of various rab proteins, we propose to rename it rab GDI.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 247 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 0 times in Scopus Article
Google Scholar Search Google Scholar
Created: Wed, 06 Aug 2014, 13:31:57 EST by System User on behalf of Learning and Research Services (UQ Library)