PortalPublikationenThe Legionella effector protein DrrA AMPylates the membrane ...

The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b

Standard

The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. / Peters, Heide; Blümer, Julia; Blankenfeldt, Wulf; Goody, Roger S; Itzen, Aymelt.

in: SCIENCE, Jahrgang 329, Nr. 5994, 20.08.2010, S. 946-9.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Peters, H, Blümer, J, Blankenfeldt, W, Goody, RS & Itzen, A 2010, 'The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b', SCIENCE, Jg. 329, Nr. 5994, S. 946-9. https://doi.org/10.1126/science.1192276

APA

Peters, H., Blümer, J., Blankenfeldt, W., Goody, R. S., & Itzen, A. (2010). The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. SCIENCE, 329(5994), 946-9. https://doi.org/10.1126/science.1192276

Vancouver

Peters H, Blümer J, Blankenfeldt W, Goody RS, Itzen A. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. SCIENCE. 2010 Aug 20;329(5994):946-9. https://doi.org/10.1126/science.1192276

Bibtex

@article{a786e340ed53462aad9ef040e45737a5,
title = "The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b",
abstract = "In the course of Legionnaires' disease, the bacterium Legionella pneumophila affects the intracellular vesicular trafficking of infected eukaryotic cells by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole. In order to accomplish this, the Legionella protein DrrA contains a specific guanine nucleotide exchange activity for Rab1 activation that exchanges guanosine triphosphate (GTP) for guanosine diphosphate on Rab1. We found that the amino-terminal domain of DrrA possesses adenosine monophosphorylation (AMPylation) activity toward the switch II region of Rab1b, leading to posttranslational covalent modification of tyrosine 77. AMPylation of switch II by DrrA restricts the access of GTPase activating proteins, thereby rendering Rab1b constitutively active.",
keywords = "Adenosine Monophosphate, Animals, Bacterial Proteins, COS Cells, Cercopithecus aethiops, Crystallography, Guanine Nucleotide Exchange Factors, Legionella pneumophila, Mass Spectrometry, Models, Molecular, Protein Structure, Tertiary, rab GTP-Binding Proteins, rab1 GTP-Binding Proteins, Journal Article, Research Support, Non-U.S. Gov't",
author = "Heide Peters and Julia Bl{\"u}mer and Wulf Blankenfeldt and Goody, {Roger S} and Aymelt Itzen",
year = "2010",
month = aug,
day = "20",
doi = "10.1126/science.1192276",
language = "English",
volume = "329",
pages = "946--9",
journal = "SCIENCE",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5994",

}

RIS

TY - JOUR

T1 - The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b

AU - Peters, Heide

AU - Blümer, Julia

AU - Blankenfeldt, Wulf

AU - Goody, Roger S

AU - Itzen, Aymelt

PY - 2010/8/20

Y1 - 2010/8/20

N2 - In the course of Legionnaires' disease, the bacterium Legionella pneumophila affects the intracellular vesicular trafficking of infected eukaryotic cells by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole. In order to accomplish this, the Legionella protein DrrA contains a specific guanine nucleotide exchange activity for Rab1 activation that exchanges guanosine triphosphate (GTP) for guanosine diphosphate on Rab1. We found that the amino-terminal domain of DrrA possesses adenosine monophosphorylation (AMPylation) activity toward the switch II region of Rab1b, leading to posttranslational covalent modification of tyrosine 77. AMPylation of switch II by DrrA restricts the access of GTPase activating proteins, thereby rendering Rab1b constitutively active.

AB - In the course of Legionnaires' disease, the bacterium Legionella pneumophila affects the intracellular vesicular trafficking of infected eukaryotic cells by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole. In order to accomplish this, the Legionella protein DrrA contains a specific guanine nucleotide exchange activity for Rab1 activation that exchanges guanosine triphosphate (GTP) for guanosine diphosphate on Rab1. We found that the amino-terminal domain of DrrA possesses adenosine monophosphorylation (AMPylation) activity toward the switch II region of Rab1b, leading to posttranslational covalent modification of tyrosine 77. AMPylation of switch II by DrrA restricts the access of GTPase activating proteins, thereby rendering Rab1b constitutively active.

KW - Adenosine Monophosphate

KW - Animals

KW - Bacterial Proteins

KW - COS Cells

KW - Cercopithecus aethiops

KW - Crystallography

KW - Guanine Nucleotide Exchange Factors

KW - Legionella pneumophila

KW - Mass Spectrometry

KW - Models, Molecular

KW - Protein Structure, Tertiary

KW - rab GTP-Binding Proteins

KW - rab1 GTP-Binding Proteins

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1126/science.1192276

DO - 10.1126/science.1192276

M3 - SCORING: Journal article

C2 - 20651120

VL - 329

SP - 946

EP - 949

JO - SCIENCE

JF - SCIENCE

SN - 0036-8075

IS - 5994

ER -