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Trends Cell Biol. 1999 Mar;9(3):107-12.

Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels.

Author information

1
Dept of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL, USA. l-hicke@nwu.edu

Abstract

G-protein-coupled receptors and transporters in Saccharomyces cerevisiae are modified with ubiquitin in response to ligand biding. In most cases, the proteasome does not recognize these ubiquitinated proteins. Instead, ubiquitination serves to trigger internalization and degradation of plasma membrane proteins in the lysosome-like vacuole. A number of mammalian receptors and at least one ion channel undergo ubiquitination at the plasma membrane, and this modification is required for their downregulation. Some of these cell-surface proteins appear to be degraded by both the proteasome and lysosomal proteases. Recent evidence indicates that other proteins required for receptor internalization might also be regulated by ubiquitination, suggesting that ubiquitin plays diverse roles in regulating plasma membrane protein activity.

PMID:
10201076
DOI:
10.1016/s0962-8924(98)01491-3
[Indexed for MEDLINE]

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