期刊
TRAFFIC
卷 3, 期 11, 页码 771-780出版社
WILEY
DOI: 10.1034/j.1600-0854.2002.31102.x
关键词
degradation; multivesicular endosome; proteasome; ubiquitylation; vps genes
类别
资金
- NIDDK NIH HHS [DK40344, DK48280] Funding Source: Medline
- NIGMS NIH HHS [GM58212] Funding Source: Medline
Exportable proteins that have significant defects in nascent polypeptide folding or subunit assembly are frequently retained in the endoplasmic reticulum and subject to endoplasmic reticulum-associated degradation by the ubiquitin-proteasome system. In addition to this, however, there is growing evidence for post-endoplasmic reticulum quality control mechanisms in which mutant or non-native exportable proteins may undergo anterograde transport to the Golgi complex and post-Golgi compartments before intracellular disposal. In some instances, these proteins may undergo retrograde transport back to the endoplasmic reticulum with re-targeting to the endoplasmic reticulum-associated degradation pathway; in other typical cases, they are targeted into the endosomal system for degradation by vacuolar/lysosomal proteases. Such quality control targeting is likely to involve recognition of features more commonly expressed in mutant proteins, but may also be expressed by wild-type proteins, especially in cells with perturbation of local environments that are essential for normal protein trafficking and stability in the secretory pathway and at the cell surface .
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