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Vol. 12, Issue 5, 1215-1226, May 2001
*Departments of Molecular Biophysics and Biochemistry and
A family of related proteins in yeast Saccharomyces
cerevisiae is known to have in vitro GTPase-activating
protein activity on the Rab GTPases. However, their in vivo
function remains obscure. One of them, Gyp1p, acts on Sec4p, Ypt1p,
Ypt7p, and Ypt51p in vitro. Here, we present data to reveal its in vivo
substrate and the role that it plays in the function of the Rab GTPase.
Red fluorescent protein-tagged Gyp1p is concentrated on cytoplasmic punctate structures that largely colocalize with a
cis-Golgi marker. Subcellular fractionation of a yeast
lysate confirmed that Gyp1p is peripherally associated with membranes
and that it cofractionates with Golgi markers. This localization
suggests that Gyp1p may only act on Rab GTPases on the Golgi. A
gyp1Cell Biology, Yale University School of Medicine, New
Haven, Connecticut 06520
strain displays a growth defect on synthetic
medium at 37°C. Overexpression of Ypt1p, but not other Rab GTPases,
strongly inhibits the growth of gyp1 cells.
Conversely, a partial loss-of-function allele of YPT1,
ypt1-2, can suppress the growth defect of
gyp1 cells. Furthermore, deletion of
GYP1 can partially suppress growth defects associated
with mutants in subunits of transport protein particle complex, a
complex that catalyzes nucleotide exchange on Ypt1p. These results
establish that Gyp1p functions on the Golgi as a negative regulator of Ypt1p.
Corresponding author: E-mail:
peter.novick{at}yale.edu.
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