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J Biol Chem, Vol. 274, Issue 3, 1835-1841, January 15, 1999
From the Department of Cell Biology and Physiology, Washington
University School of Medicine, St. Louis, Missouri 63110
G protein-coupled receptors that transduce
signals for many hormones, neurotransmitters, and inflammatory
mediators are internalized and subsequently recycled to the plasma
membrane, or down-regulated by targeting to lysosomes for degradation.
Here we have characterized yeast
A Syntaxin Homolog Encoded by VAM3 Mediates
Down-regulation of a Yeast G Protein-coupled Receptor
-factor receptors tagged with green
fluorescent protein (Ste2-GFP) and used them to obtain mutants
defective in receptor down-regulation. In wild type cells, Ste2-GFP was
functional and localized to the plasma membrane and endocytic
compartments. Although GFP was fused to the cytoplasmic tail of the
receptor, GFP also accumulated in the lumen of the vacuole, suggesting
that the receptor's extracellular and cytoplasmic domains are degraded
within the vacuole lumen. Transposon mutagenesis and a visual screen
were used to identify mutants displaying aberrant localization of
Ste2-GFP. Mutants that accumulated Ste2-GFP in numerous intracellular
vesicles carried disruptions of the VAM3/PTH1 gene, which
encodes a syntaxin homolog (t-SNARE) required for homotypic vacuole
membrane fusion, autophagy and fusion of biosynthetic transport
vesicles with the vacuole. We provide evidence that Vam3 is required
for the delivery of -factor receptor-ligand complexes to the
vacuole. Vam3 homologs in mammalian cells may mediate late steps in the
down-regulation and lysosomal degradation pathways of various G
protein-coupled receptors.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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