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Molecular and Cellular Biology, February 2002, p. 927-934, Vol. 22, No. 3
0270-7306/01/$04.00+0     DOI: 10.1128/MCB.22.3.927-934.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The Sur7p Family Defines Novel Cortical Domains in Saccharomyces cerevisiae, Affects Sphingolipid Metabolism, and Is Involved in Sporulation

Michael E. Young,1 Tatiana S. Karpova,1 Britta Brügger,2 Darcy M. Moschenross,1 Georgeann K. Wang,1 Roger Schneiter,3 Felix T. Wieland,2 and John A. Cooper1*

Department of Cell Biology and Physiology, Washington University, St. Louis, Missouri 63110,1 Biochemie-Zentrum Heidelberg, Ruprecht-Karls-Universität Heidelberg, 69120 Heidelberg, Germany,2 Department of Biochemistry, Graz University of Technology, 8010 Graz, Austria3

Received 3 May 2001/ Returned for modification 5 July 2001/ Accepted 5 November 2001

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{Delta}, ydl222{Delta}, and ynl194{Delta} 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 sur7{Delta}, ydl222{Delta}, and yne194{Delta} strains.

* Corresponding author. Mailing address: Department of Cell Biology and Physiology, Washington University, Box 8228, 660 S. Euclid Ave., St. Louis, MO 63110. Phone: (314) 362-3964. Fax: (314) 362-0098. E-mail: jcooper{at}cellbio.wustl.edu.

Molecular and Cellular Biology, February 2002, p. 927-934, Vol. 22, No. 3
0022-538X/01/$04.00+0     DOI: 10.1128/MCB.22.3.927-934.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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