De-AMPylation of the Small GTPase Rab1 by the Pathogen Legionella pneumophila-Reference-Cited by-同舟云学术

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

Published:2011-07-22 Issue:6041 Volume:333 Page:453-456
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Neunuebel M. Ramona¹,Chen Yang¹²,Gaspar Andrew H.¹,Backlund Peter S.³,Yergey Alfred³,Machner Matthias P.¹

Affiliation:

1. Cell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.

2. Health Science Center, Peking University, Beijing 100191, China.

3. Biomedical Mass Spectrometry Facility, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.

Abstract

A bacterial pathogen reverses the modification of a host cell protein involved in membrane trafficking.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference27 articles.

1. AMPylation of Rho GTPases by Vibrio VopS Disrupts Effector Binding and Downstream Signaling

2. The Fic Domain: Regulation of Cell Signaling by Adenylylation

3. The Legionella Effector Protein DrrA AMPylates the Membrane Traffic Regulator Rab1b

4. Legionella pneumophila Dot/Icm translocated substrates: a sum of parts

5. The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor

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