Exoenzyme S from P-aeruginosa ADP ribosylates rab4 and inhibits transferrin recycling in SLO-permeabilized reticulocytes

被引：18

作者：

Bette-Bobillo, P ^{[1
]}

Giro, P ^{[1
]}

Sainte-Marie, J ^{[1
]}

Vidal, M ^{[1
]}

机构：

[1] Univ Montpellier 2, UMR 5539 CNRS, F-34095 Montpellier, France

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 244卷 / 02期

关键词：

D O I：

10.1006/bbrc.1998.8263

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：

ADP-ribosylation of rab proteins by exoenzyme S (Exo S) of P. aeruginosa was studied using reticulocytes. 14-3-3 protein, the eukaryotic cofactor that is obligatory for fro S activity, was found in association with reticulocyte endocytic vesicles and exosomes, vesicles previously shown to be enriched with rab4. Incubation of purified endocytic vesicles with fro S triggered rab4 ADP-ribosylation. Transferrin recycling in SLO-permeabilized reticulocytes was highly impaired when Exo S was added to the cells, suggesting that ADP-ribosylation affected rab4 function. Moreover, in vitro ADP-ribosylation of different rab proteins was studied using the cofactor activity extracted from reticulocytes. (C) 1998 Academic Press.

引用

页码：336 / 341

页数：6

共 27 条

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