Abstract
The regulation of membrane traffic involves the Rab family of Ras-related GTPases, of which there are a total of 11 members in the yeast Saccharomyces cerevisiae. Previous work has identified PRA1 as a dual prenylated Rab GTPase and VAMP2 interacting protein [Martinic et al. (1999) J. Biol. Chem. 272, 26991-26998]. In this study we demonstrate that the yeast counterpart of PRA1 interacts with Rab proteins and with Yip1p, a membrane protein of unknown function that has been reported to interact specifically with the Rab proteins Ypt1p and Ypt31p. Yeast Pra1p/Yip3p is a factor capable of biochemical interaction with a panel of different Rab proteins and does not show in vitro specificity for any particular Rab. The interactions between Pra1p/Yip3p and Rab proteins are dependent on the presence of the Rab protein C-terminal cysteines and require C-terminal prenylation.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
-
Blotting, Western
-
Electrophoresis, Polyacrylamide Gel
-
Fungal Proteins / genetics
-
Fungal Proteins / metabolism*
-
Membrane Proteins
-
Protein Binding / physiology
-
Receptors, Cell Surface*
-
Recombinant Fusion Proteins / genetics
-
Recombinant Fusion Proteins / metabolism
-
Saccharomyces cerevisiae
-
Saccharomyces cerevisiae Proteins
-
Two-Hybrid System Techniques
-
Vesicular Transport Proteins
-
rab GTP-Binding Proteins / genetics
-
rab GTP-Binding Proteins / metabolism*
-
rab1 GTP-Binding Proteins / metabolism
-
rab5 GTP-Binding Proteins / metabolism
Substances
-
Fungal Proteins
-
Membrane Proteins
-
Receptors, Cell Surface
-
Recombinant Fusion Proteins
-
Saccharomyces cerevisiae Proteins
-
Vesicular Transport Proteins
-
Yip1 protein, S cerevisiae
-
rab GTP-Binding Proteins
-
rab1 GTP-Binding Proteins
-
rab5 GTP-Binding Proteins