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First published online January 12, 2006

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ATPase escapes ubiquitylation by raft

Many cell-surface proteins reside only briefly at the plasma membrane before being ubiquitylated and internalized. In yeast, however, the plasma membrane ATPase Pma1 somehow stays at the cell surface for many hours. One way it might do so is through association with detergent-insoluble glycolipid complexes (DIGs, also known as lipid rafts). On p. 360, Yu Liu and Amy Chang provide new support for this hypothesis by investigating how Pma1-10, a temperature-sensitive mutant of Pma1, is rapidly removed from the plasma membrane. They show that at the restrictive temperature Pma1-10, unlike Pma1, is ubiquitylated before or upon arrival at the plasma membrane and then rapidly internalized by the endocytic machinery. Unexpectedly, ubiquitylation of Pma1-10 is reversed when endocytosis is blocked and the misfolded protein then associates with DIGs. Other results lead Liu and Chang to propose a quality-control mechanism in which ubiquitylation, by targeting misfolded Pma1-10 for rapid removal from the plasma membrane, preempts the establishment of the interaction with DIGs that normally stabilizes Pma1 at the cell surface.

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Related articles in JCS:

Quality control of a mutant plasma membrane ATPase: ubiquitylation prevents cell-surface stability

Yu Liu and Amy Chang
JCS 2006 119: 360-369. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?