Affiliation:
1. Department of Cell Biology and Physiology, Washington University, St. Louis, Missouri 63110
2. Biochemie-Zentrum Heidelberg, Ruprecht-Karls-Universität Heidelberg, 69120 Heidelberg, Germany
Abstract
ABSTRACT
We have discovered a novel cortical patch structure in
Saccharomyces cerevisiae
defined by a family of integral plasma membrane proteins, including Sur7p, Ynl194p, and Ydl222p. Sur7p-family patches localized as cortical patches that were immobile and stable. These patches were polarized to regions of the cell with a mature cell wall; they were absent from small buds and the tips of many medium-sized buds. These patches were distinct from other known cortical structures. Digestion of the cell wall caused Sur7p patches to disassemble, indicating that Sur7p requires cell wall-dependent extracellular interactions for its localization as patches.
sur7
Δ,
ydl222
Δ, and
ynl194
Δ mutants had reduced sporulation efficiencies.
SUR7
was originally described as a multicopy suppressor of
rvs167
, whose product is an actin patch component. This suppression is probably mediated by sphingolipids, since deletion of
SUR7
,
YDL222
, and
YNL194
altered the sphingolipid content of the yeast plasma membrane, and other
SUR
genes suppress
rvs167
via effects on sphingolipid synthesis. In particular, the sphingoid base length and number of hydroxyl groups in inositolphosphorylceramides were altered in
sur
7Δ,
ydl222
Δ, and
yne194
Δ strains.
Publisher
American Society for Microbiology
Subject
Cell Biology,Molecular Biology
Cited by
111 articles.
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