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MBC in Press, published online ahead of print July 25, 2003
Mol. Biol. Cell 10.1091/mbc.E03-04-0221

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Submitted on April 10, 2003
Revised on June 3, 2003
Accepted on June 26, 2003

Visualization of protein compartmentation within the plasma membrane of living yeast cells

K. Malínská1, J. Malínsky2, M. Opekarová3, and W. Tanner1*

1 Universität Regensburg, Lehrstuhl für Zellbiologie und Pflanzenphysiologie, 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, 14220 Prague 4, Czech Republic

* Corresponding author. E-mail address: sekretariat.tanner{at}biologie.uni-regensburg.de.

Different distribution patterns of the arginine/H+ symporter Can1p, the H+ plasma membrane ATPase Pma1p, and the hexose transport facilitator Hxt1p within the plasma membrane of living S. cerevisiae cells were visualized using fluorescence-protein tagging of these proteins. While Hxt1p-GFP was evenly distributed through the whole cell surface, Can1p-GFP and Pma1p-GFP were confined to characteristic subregions in the plasma membrane. Pma1p is a well-documented raft protein. Evidence is presented that Can1p, but not Hxt1p, is exclusively associated with lipid rafts, too. Double labeling experiments with Can1p-GFP and Pma1p-RFP containing cells demonstrate that these proteins occupy two different nonoverlapping membrane microdomains. The size of Can1p-rich (Pma1p-poor) areas was estimated to 300 nm. These domains were shown to be stable in growing cells for more than 30 min. To our knowledge, this is the first observation of a cell polarization-independent lateral compartmentation in the plasma membrane of a living cell.




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