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First published online 9 November 2004
doi: 10.1242/jcs.01493

Journal of Cell Science 117, 6031-6041 (2004)
Published by The Company of Biologists 2004
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Research Article

Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of living S. cerevisiae cells

Katerina Malinska1,*, Jan Malinsky2, Miroslava Opekarova3 and Widmar Tanner1,{ddagger}

1 Universität Regensburg, Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universitätsstrasse 31, 93040 Regensburg, Germany
2 Institute of Experimental Medicine, CAS, and 1st Faculty of Medicine, Charles University, Albertov 4, 12801 Prague 2, Czech Republic
3 Institute of Microbiology, CAS, Videnska 1083, 14220 Prague 4, Czech Republic

{ddagger} Author for correspondence (e-mail: sekretariat.tanner{at}biologie.uni-regensburg.de)

Accepted 16 August 2004

Recently, lipid-raft-based subdomains within the plasma membrane of living Saccharomyces cerevisiae cells were visualized using green fluorescent protein fusions, and non-overlapping subdomains containing either Pma1p or Can1p were distinguished. In this study, the long-term stability of the subdomains was investigated. Experiments with latrunculin A and nocodazole ruled out the involvement of cytoskeletal components in the stabilization of the subdomains. Also a putative role of the cell wall was excluded, because protoplasting of the cells changed neither the pattern nor the stability of the subdomains. By contrast, the expected inner dynamics of the membrane subdomains was documented by FRAP experiments. Finally, two other proteins were localized within the frame of the Can1p/Pma1p plasma-membrane partition. We show that Fur4p (another H+ symporter) and Sur7p (a protein of unknown function) occupy the Can1p subdomain.

Key words: Lipid rafts, CAN1, FUR4, SUR7, PMA1


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