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Vol. 11, Issue 7, 2429-2443, July 2000
Department of Biological Sciences, Stanford University, Stanford,
California 94305-5020
We have characterized LUV1/RKI1/TCS3/VPS54, a novel
yeast gene required to maintain normal vacuolar morphology. The
luv1 mutant was identified in a genetic screen for
mutants requiring the phosphatase calcineurin for vegetative growth.
luv1 mutants lack a morphologically intact vacuole and
instead accumulate small vesicles that are acidified and contain the
vacuolar proteins alkaline phosphatase and carboxypeptidase Y and the
vacuolar membrane H+-ATPase. Endocytosis appears
qualitatively normal in luv1 mutants, but some portion
(28%) of carboxypeptidase Y is secreted. luv1 mutants
are sensitive to several ions (Zn2+, Mn2+, and
Cd2+) and to pH extremes. These mutants are also sensitive
to hygromycin B, caffeine, and FK506, a specific inhibitor of
calcineurin. Some vacuolar protein-sorting mutants display similar drug
and ion sensitivities, including sensitivity to FK506. Luv1p sediments at 100,000 × g and can be solubilized by salt or
carbonate, indicating that it is a peripheral membrane protein. A Green
Fluorescent Protein-Luv1 fusion protein colocalizes with the dye FM
4-64 at the endosome, and hemagglutinin-tagged Luv1p colocalizes with the trans-Golgi network/endosomal protease Kex2p.
Computer analysis predicts a short coiled-coil domain in Luv1p. We
propose that this protein maintains traffic through or the integrity of
the early endosome and that this function is required for proper
vacuolar morphology.
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