PMID- 10637310
OWN - NLM
STAT- MEDLINE
DCOM- 20000407
LR  - 20181130
IS  - 1059-1524 (Print)
IS  - 1059-1524 (Linking)
VI  - 11
IP  - 1
DP  - 2000 Jan
TI  - Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein
      sorting at the yeast late Golgi.
PG  - 305-23
AB  - The late Golgi of the yeast Saccharomyces cerevisiae receives membrane traffic
      from the secretory pathway as well as retrograde traffic from post-Golgi
      compartments, but the machinery that regulates these vesicle-docking and fusion
      events has not been characterized. We have identified three components of a novel
      protein complex that is required for protein sorting at the yeast late Golgi
      compartment. Mutation of VPS52, VPS53, or VPS54 results in the missorting of 70% 
      of the vacuolar hydrolase carboxypeptidase Y as well as the mislocalization of
      late Golgi membrane proteins to the vacuole, whereas protein traffic through the 
      early part of the Golgi complex is unaffected. A vps52/53/54 triple mutant strain
      is phenotypically indistinguishable from each of the single mutants, consistent
      with the model that all three are required for a common step in membrane
      transport. Native coimmunoprecipitation experiments indicate that Vps52p, Vps53p,
      and Vps54p are associated in a 1:1:1 complex that sediments as a single peak on
      sucrose velocity gradients. This complex, which exists both in a soluble pool and
      as a peripheral component of a membrane fraction, colocalizes with markers of the
      yeast late Golgi by immunofluorescence microscopy. Together, the phenotypic and
      biochemical data suggest that VPS52, VPS53, and VPS54 are required for the
      retrograde transport of Golgi membrane proteins from an endosomal/prevacuolar
      compartment. The Vps52/53/54 complex joins a growing list of distinct
      multisubunit complexes that regulate membrane-trafficking events.
FAU - Conibear, E
AU  - Conibear E
AD  - Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403-1229, 
      USA.
FAU - Stevens, T H
AU  - Stevens TH
LA  - eng
GR  - R01 GM032448/GM/NIGMS NIH HHS/United States
GR  - R37 GM032448/GM/NIGMS NIH HHS/United States
GR  - GM32448/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Biol Cell
JT  - Molecular biology of the cell
JID - 9201390
RN  - 0 (Carrier Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (PEP1 protein, S cerevisiae)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (VPS52 protein, S cerevisiae)
RN  - 0 (VPS53 protein, S cerevisiae)
RN  - 0 (VPS54 protein, S cerevisiae)
RN  - 0 (Vesicular Transport Proteins)
RN  - EC 3.1.3.1 (Alkaline Phosphatase)
RN  - EC 3.2.1.- (Glycoside Hydrolases)
RN  - EC 3.2.1.26 (beta-Fructofuranosidase)
SB  - IM
MH  - Alkaline Phosphatase/metabolism
MH  - *Carrier Proteins
MH  - Cell Compartmentation
MH  - Cloning, Molecular
MH  - Fungal Proteins/genetics/*metabolism
MH  - Genes, Fungal
MH  - Glycoside Hydrolases/metabolism
MH  - Glycosylation
MH  - Golgi Apparatus/*metabolism
MH  - Intracellular Membranes/metabolism
MH  - Membrane Proteins/metabolism
MH  - Mutagenesis
MH  - Receptors, Cell Surface/metabolism
MH  - Saccharomyces cerevisiae/genetics/*metabolism
MH  - *Saccharomyces cerevisiae Proteins
MH  - Vacuoles/metabolism
MH  - *Vesicular Transport Proteins
MH  - beta-Fructofuranosidase
PMC - PMC14776
EDAT- 2000/01/19 00:00
MHDA- 2000/01/19 00:01
CRDT- 2000/01/19 00:00
PHST- 2000/01/19 00:00 [pubmed]
PHST- 2000/01/19 00:01 [medline]
PHST- 2000/01/19 00:00 [entrez]
AID - 10.1091/mbc.11.1.305 [doi]
PST - ppublish
SO  - Mol Biol Cell. 2000 Jan;11(1):305-23. doi: 10.1091/mbc.11.1.305.