DOI: 10.1242/jcs.01493. Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of living<i>S. cerevisiae</i>cells

Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of livingS. cerevisiaecells

10.1242/jcs.01493

Crossref journal-article

The Company of Biologists

Journal of Cell Science (237)

Abstract

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.

Bibliography

Malinska, K., Malinsky, J., Opekarova, M., & Tanner, W. (2004). Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of livingS. cerevisiaecells. Journal of Cell Science, 117(25), 6031â6041.

Authors 4

Katerina Malinska (first)
Jan Malinsky (additional)
Miroslava Opekarova (additional)
Widmar Tanner (additional)

References 38 Referenced 140

Dates

Type	When
Created	20 years, 9 months ago (Nov. 9, 2004, 9:48 p.m.)
Deposited	4 years, 2 months ago (June 27, 2021, 10:12 p.m.)
Indexed	3 weeks, 5 days ago (Aug. 3, 2025, 6:53 p.m.)
Issued	20 years, 8 months ago (Dec. 1, 2004)
Published	20 years, 8 months ago (Dec. 1, 2004)
Published Print	20 years, 8 months ago (Dec. 1, 2004)

Funders 0

None

BibTeX

@article{Malinska_2004, title={Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of livingS. cerevisiaecells}, volume={117}, ISSN={0021-9533}, url={http://dx.doi.org/10.1242/jcs.01493}, DOI={10.1242/jcs.01493}, number={25}, journal={Journal of Cell Science}, publisher={The Company of Biologists}, author={Malinska, Katerina and Malinsky, Jan and Opekarova, Miroslava and Tanner, Widmar}, year={2004}, month=dec, pages={6031–6041} }

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  "abstract": "<jats:p>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.</jats:p>",
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