TY - JOUR
T1 - Rab GDP dissociation inhibitor as a general regulator for the membrane association of Rab proteins
AU - Ullrich, Oliver
AU - Stenmark, Harald
AU - Alexandrov, Kirill
AU - Huber, Lukas A.
AU - Kaibuchi, Kozo
AU - Sasaki, Takuya
AU - Takai, Yoshimi
AU - Zerial, Marino
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1993/8/25
Y1 - 1993/8/25
N2 - 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 p25 A/ 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.
AB - 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 p25 A/ 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.
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U2 - 10.1016/s0021-9258(17)46822-0
DO - 10.1016/s0021-9258(17)46822-0
M3 - Article
C2 - 8349690
AN - SCOPUS:0027202199
SN - 0021-9258
VL - 268
SP - 18143
EP - 18150
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 24
ER -