De-AMPylation of the Small GTPase Rab1 by the Pathogen Legionella pneumophila

被引：180

作者：

Neunuebel, M. Ramona ^{[1
]}

Chen, Yang ^{[1
,3
]}

Gaspar, Andrew H. ^{[1
]}

Backlund, Peter S., Jr. ^{[2
]}

Yergey, Alfred ^{[2
]}

Machner, Matthias P. ^{[1
]}

机构：

[1] Eunice Kennedy Shriver Natl Inst Child Hlth & Hum, Cell Biol & Metab Program, NIH, Bethesda, MD 20892 USA

[2] Eunice Kennedy Shriver Natl Inst Child Hlth & Hum, Biomed Mass Spectrometry Facil, NIH, Bethesda, MD 20892 USA

[3] Peking Univ, Ctr Hlth Sci, Beijing 100191, Peoples R China

来源：

SCIENCE | 2011年 / 333卷 / 6041期

关键词：

EFFECTOR PROTEIN DRRA; ENDOPLASMIC-RETICULUM; VESICULAR TRANSPORT; BINDING; SYSTEM; MUTANTS;

D O I：

10.1126/science.1207193

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The bacterial pathogen Legionella pneumophila exploits host cell vesicle transport by transiently manipulating the activity of the small guanosine triphosphatase (GTPase) Rab1. The effector protein SidM recruits Rab1 to the Legionella-containing vacuole (LCV), where it activates Rab1 and then AMPylates it by covalently adding adenosine monophosphate (AMP). L. pneumophila GTPase-activating protein LepB inactivates Rab1 before its removal from LCVs. Because LepB cannot bind AMPylated Rab1, the molecular events leading to Rab1 inactivation are unknown. We found that the effector protein SidD from L. pneumophila catalyzed AMP release from Rab1, generating de-AMPylated Rab1 accessible for inactivation by LepB. L. pneumophila mutants lacking SidD were defective for Rab1 removal from LCVs, identifying SidD as the missing link connecting the processes of early Rab1 accumulation and subsequent Rab1 removal during infection.

引用

页码：453 / 456

页数：4

共 20 条

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