Abstract
Yeast permeases, that act as transporters for nutrients including amino acids, nucleobases and metals, provide a powerful model system for dissecting the physiological control of membrane protein trafficking. Modification of these transporters by ubiquitin is known to target them for degradation in the vacuole, the degradation organelle of fungi. Recent studies have uncovered the role of specific adaptors for recruiting the Rsp5 ubiquitin ligase to these proteins. In addition, the role of ubiquitin at different trafficking steps including early endocytosis, sorting into the multivesicular body (MVB) pathway and Golgi-to-endosome transit is now becoming clear. In particular, K63-linked ubiquitin chains now emerge as a specific signal for protein sorting into the MVB pathway. A complete view of the ubiquitin code governing yeast permease trafficking might not be far off.
Copyright 2010 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Endocytosis
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Endosomal Sorting Complexes Required for Transport / genetics
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Endosomal Sorting Complexes Required for Transport / metabolism
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Gene Expression Regulation, Enzymologic*
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Humans
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Membrane Transport Proteins / genetics
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Membrane Transport Proteins / metabolism*
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Multivesicular Bodies / metabolism
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Protein Transport / physiology*
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism
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Ubiquitin / metabolism*
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Ubiquitin-Protein Ligase Complexes / genetics
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Ubiquitin-Protein Ligase Complexes / metabolism
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Vacuoles / metabolism
Substances
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Endosomal Sorting Complexes Required for Transport
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Membrane Proteins
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Membrane Transport Proteins
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Saccharomyces cerevisiae Proteins
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Ubiquitin
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Ubiquitin-Protein Ligase Complexes
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RSP5 protein, S cerevisiae