UBIQUITINATED PROTEIN CONJUGATES ARE SPECIFICALLY ENRICHED IN THE LYSOSOMAL SYSTEM OF FIBROBLASTS

被引：91

作者：

LASZLO, L ^{[1
]}

DOHERTY, FJ ^{[1
]}

OSBORN, NU ^{[1
]}

MAYER, RJ ^{[1
]}

机构：

[1] EOTVOS LORAND TUG EGYET,DEPT GEN ZOOL,H-1088 BUDAPEST,HUNGARY

来源：

FEBS LETTERS | 1990年 / 261卷 / 02期

关键词：

(3T3-L1 fibroblasts); Electron microscopy; Epoxysuccinyl-leucylamido-(4-guanadino)butane; Lysosome; Ubiquitin;

D O I：

10.1016/0014-5793(90)80593-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Ubiquitin-protein conjugates are found by imniunogold electron microscopy to be enriched (12-fold) in the lysosomal compartment of 3T3-L1 fibroblasts. Treatment of fibroblasts with the cysteine protease inhibitor E-64 leads to an expansion of the lysosomal compartment and as a result an increase in the cellular content of ubiquitin-protein conjugates. There is no change in the specific enrichment of ubiquitin-protein conjugates in the lysosomal compartment following E-64 treatment. The results suggest that some ubiquitin-protein conjugates may normally be degraded lysosomally following sequestration by microautophagy and imply that protein ubiquitination may be one of the signals for protein uptake into lysosomes. © 1990.

引用

页码：365 / 368

页数：4

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