Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of living S. cerevisiae cells.
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.
Malinska
Katerina
K
Universität Regensburg, Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universitätsstrasse 31, 93040 Regensburg, Germany.
Malinsky
Jan
J
Opekarova
Miroslava
M
Tanner
Widmar
W
D000199:Actins / Q000737:chemistry / Q000378:metabolism; D026905:Amino Acid Transport Systems / Q000378:metabolism*; D026923:Amino Acid Transport Systems, Basic / Q000378:metabolism*; D000970:Antineoplastic Agents / Q000494:pharmacology; D019086:Bridged Bicyclo Compounds, Heterocyclic / Q000494:pharmacology; D002462:Cell Membrane / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism; D002875:Chromosomes / Q000378:metabolism; D003001:Cloning, Molecular; D003599:Cytoskeleton / Q000378:metabolism; D004247:DNA / Q000378:metabolism; D003902:Detergents / Q000494:pharmacology; D005656:Fungal Proteins / Q000378:metabolism*; D005838:Genotype; D049452:Green Fluorescent Proteins / Q000378:metabolism; D015151:Immunoblotting; D008387:Marine Toxins / Q000494:pharmacology; D021962:Membrane Microdomains / Q000378:metabolism; D008565:Membrane Proteins / Q000096:biosynthesis* / Q000737:chemistry; D015739:Nocodazole / Q000494:pharmacology; D033704:Nucleotide Transport Proteins / Q000378:metabolism; D017830:Octoxynol / Q000494:pharmacology; D010957:Plasmids / Q000378:metabolism; D017434:Protein Structure, Tertiary; D006180:Proton-Translocating ATPases / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000378:metabolism*; D013844:Thiazoles / Q000494:pharmacology; D053778:Thiazolidines; D013997:Time Factors
D000199:Actins; D026905:Amino Acid Transport Systems; D026923:Amino Acid Transport Systems, Basic; D000970:Antineoplastic Agents; D019086:Bridged Bicyclo Compounds, Heterocyclic; C097640:CAN1 protein, Candida albicans; C502212:CAN1 protein, S cerevisiae; D003902:Detergents; C035528:FUR4 protein, S cerevisiae; D005656:Fungal Proteins; D008387:Marine Toxins; D008565:Membrane Proteins; D033704:Nucleotide Transport Proteins; C502213:SUR7 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D013844:Thiazoles; D053778:Thiazolidines; D049452:Green Fluorescent Proteins; D017830:Octoxynol; D004247:DNA; C092477:PMA1 protein, S cerevisiae; D006180:Proton-Translocating ATPases; D015739:Nocodazole; C037067:latrunculin A