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Vol. 12, Issue 1, 13-26, January 2001
Department of Biological Chemistry, University of California, Los
Angeles, Los Angeles, California 90095-3717
In Saccharomyces cerevisiae, clathrin is necessary
for localization of trans-Golgi network (TGN) membrane
proteins, a process that involves cycling of TGN proteins between the
TGN and endosomes. To characterize further TGN protein localization, we
applied a screen for mutations that cause severe growth defects in
combination with a temperature-sensitive clathrin heavy chain. This
screen yielded a mutant allele of RIC1. Cells carrying a
deletion of RIC1 (ric1
) mislocalize
TGN membrane proteins Kex2p and Vps10p to the vacuole. Delivery to the
vacuole occurs in ric1 cells also harboring
end3 to block endocytosis, indicative of a defect in
retrieval to the TGN rather than sorting to endosomes.
SYS1, originally discovered as a multicopy suppressor of
defects caused by the absence of the Rab GTPase YPT6,
was identified as a multicopy suppressor of ric1.
Further comparison of ric1 and ypt6
cells demonstrated identical phenotypes. Multicopy plasmids expressing v-SNAREs Gos1p or Ykt6p, but not other v- and t-SNAREs, partially suppressed phenotypes of ric1 and
ypt6 cells. SLY1-20, a dominant activator of the cis-Golgi network t-SNARE Sed5p, also
functioned as a multicopy suppressor. Because Gos1p and Ykt6p interact
with Sed5p, these results raise the possibility that TGN membrane
protein localization requires Ric1p- and Ypt6p-dependent retrieval to the cis-Golgi network.
Corresponding author. E-mail address:
gpayne{at}mednet.ucla.edu.
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