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Mol. Cell. Biol. Sep (2005); 25(17):7696-710
Immunoisolaton of the yeast Golgi subcompartments and characterization of a novel membrane protein, Svp26, discovered in the Sed5-containing compartments-
Inadome H, Noda Y, Adachi H, Yoda K
Department of Biotechnology, University of Tokyo, Japan-
Abstract: The Golgi apparatus consists of a set of vesicular compartments which are distinguished by their marker proteins- These compartments are physically separated in the Saccharomyces cerevisiae cell- To characterize them extensively, we immunoisolated vesicles carrying either of the SNAREs Sed5 or Tlg2, the markers of the early and late Golgi compartments, respectively, and analyzed the membrane proteins- The composition of proteins was mostly consistent with the position of each compartment in the traffic- We found six uncharacterized but evolutionarily conserved proteins and named them Svp26 -Sed5 compartment vesicle protein of 26 kDa-, Tvp38, Tvp23, Tvp18, Tvp15 -Tlg2 compartment vesicle proteins of 38, 23, 18, and 15 kDa-, and Gvp36 -Golgi vesicle protein of 36 kDa-- The localization of Svp26 in the early Golgi compartment was confirmed by microscopic and biochemical means- Immunoprecipitation indicated that Svp26 binds to itself and a Golgi mannosyltransferase, Ktr3- In the absence of Svp26, a considerable portion of Ktr3 was mislocalized in the endoplasmic reticulum- Our data suggest that Svp26 has a novel role in retention of a subset of membrane proteins in the early Golgi compartments-
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Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.