The ubiquitin code of yeast permease trafficking

被引：201

作者：

Lauwers, Elsa ^{[2
]}

Erpapazoglou, Zoi ^{[1
]}

Haguenauer-Tsapis, Rosine ^{[1
]}

Andre, Bruno ^{[2
]}

机构：

[1] Univ Paris Diderot, CNRS, UMR 7592, Inst Jacques Monod, F-75205 Paris 13, France

[2] Univ Libre Bruxelles, IBMM, B-6041 Gosselies, Belgium

来源：

TRENDS IN CELL BIOLOGY | 2010年 / 20卷 / 04期

关键词：

ABC-TRANSPORTER STE6; PLASMA-MEMBRANE; BINDING DOMAINS; DOWN-REGULATION; EGF RECEPTOR; DEPENDENT TRAFFICKING; POLYUBIQUITIN CHAINS; TRYPTOPHAN PERMEASE; SORTING COMPLEX; PROTEIN LIGASE;

D O I：

10.1016/j.tcb.2010.01.004

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

引用

页码：196 / 204

页数：9

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