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RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity

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RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity. / Schoebel, Stefan; Oesterlin, Lena Katharina; Blankenfeldt, Wulf; Goody, Roger Sidney; Itzen, Aymelt.

In: MOL CELL, Vol. 36, No. 6, 25.12.2009, p. 1060-72.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Schoebel, S, Oesterlin, LK, Blankenfeldt, W, Goody, RS & Itzen, A 2009, 'RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity', MOL CELL, vol. 36, no. 6, pp. 1060-72. https://doi.org/10.1016/j.molcel.2009.11.014

APA

Schoebel, S., Oesterlin, L. K., Blankenfeldt, W., Goody, R. S., & Itzen, A. (2009). RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity. MOL CELL, 36(6), 1060-72. https://doi.org/10.1016/j.molcel.2009.11.014

Vancouver

Schoebel S, Oesterlin LK, Blankenfeldt W, Goody RS, Itzen A. RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity. MOL CELL. 2009 Dec 25;36(6):1060-72. https://doi.org/10.1016/j.molcel.2009.11.014

Bibtex

@article{10b8d732a3cb4a2bb4051f889b68cbfa,
title = "RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity",
abstract = "Prenylated Rab proteins exist in the cytosol as soluble, high-affinity complexes with GDI that need to be disrupted for membrane attachment and targeting of Rab proteins. The Legionella pneumophila protein DrrA displaces GDI from Rab1:GDI complexes, incorporating Rab1 into Legionella-containing vacuoles and activating Rab1 by exchanging GDP for GTP. Here, we present the crystal structure of a complex between the GEF domain of DrrA and Rab1 and a detailed kinetic analysis of this exchange. DrrA efficiently catalyzes nucleotide exchange and mimics the general nucleotide exchange mechanism of mammalian GEFs for Ras-like GTPases. We show that the GEF activity of DrrA is sufficient to displace prenylated Rab1 from the Rab1:GDI complex. Thus, apparent GDI displacement by DrrA is linked directly to nucleotide exchange, suggesting a basic model for GDI displacement and specificity of Rab localization that does not require discrete GDI displacement activity.",
keywords = "Bacterial Proteins, Crystallography, X-Ray, DNA-Binding Proteins, Guanine Nucleotide Dissociation Inhibitors, Guanine Nucleotide Exchange Factors, Guanosine Diphosphate, Guanosine Triphosphate, Humans, Legionella pneumophila, Models, Molecular, Molecular Sequence Data, Multiprotein Complexes, Protein Binding, Protein Conformation, rab1 GTP-Binding Proteins, Journal Article",
author = "Stefan Schoebel and Oesterlin, {Lena Katharina} and Wulf Blankenfeldt and Goody, {Roger Sidney} and Aymelt Itzen",
note = "2009 Elsevier Inc.",
year = "2009",
month = dec,
day = "25",
doi = "10.1016/j.molcel.2009.11.014",
language = "English",
volume = "36",
pages = "1060--72",
journal = "MOL CELL",
issn = "1097-2765",
publisher = "Cell Press",
number = "6",

}

RIS

TY - JOUR

T1 - RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity

AU - Schoebel, Stefan

AU - Oesterlin, Lena Katharina

AU - Blankenfeldt, Wulf

AU - Goody, Roger Sidney

AU - Itzen, Aymelt

N1 - 2009 Elsevier Inc.

PY - 2009/12/25

Y1 - 2009/12/25

N2 - Prenylated Rab proteins exist in the cytosol as soluble, high-affinity complexes with GDI that need to be disrupted for membrane attachment and targeting of Rab proteins. The Legionella pneumophila protein DrrA displaces GDI from Rab1:GDI complexes, incorporating Rab1 into Legionella-containing vacuoles and activating Rab1 by exchanging GDP for GTP. Here, we present the crystal structure of a complex between the GEF domain of DrrA and Rab1 and a detailed kinetic analysis of this exchange. DrrA efficiently catalyzes nucleotide exchange and mimics the general nucleotide exchange mechanism of mammalian GEFs for Ras-like GTPases. We show that the GEF activity of DrrA is sufficient to displace prenylated Rab1 from the Rab1:GDI complex. Thus, apparent GDI displacement by DrrA is linked directly to nucleotide exchange, suggesting a basic model for GDI displacement and specificity of Rab localization that does not require discrete GDI displacement activity.

AB - Prenylated Rab proteins exist in the cytosol as soluble, high-affinity complexes with GDI that need to be disrupted for membrane attachment and targeting of Rab proteins. The Legionella pneumophila protein DrrA displaces GDI from Rab1:GDI complexes, incorporating Rab1 into Legionella-containing vacuoles and activating Rab1 by exchanging GDP for GTP. Here, we present the crystal structure of a complex between the GEF domain of DrrA and Rab1 and a detailed kinetic analysis of this exchange. DrrA efficiently catalyzes nucleotide exchange and mimics the general nucleotide exchange mechanism of mammalian GEFs for Ras-like GTPases. We show that the GEF activity of DrrA is sufficient to displace prenylated Rab1 from the Rab1:GDI complex. Thus, apparent GDI displacement by DrrA is linked directly to nucleotide exchange, suggesting a basic model for GDI displacement and specificity of Rab localization that does not require discrete GDI displacement activity.

KW - Bacterial Proteins

KW - Crystallography, X-Ray

KW - DNA-Binding Proteins

KW - Guanine Nucleotide Dissociation Inhibitors

KW - Guanine Nucleotide Exchange Factors

KW - Guanosine Diphosphate

KW - Guanosine Triphosphate

KW - Humans

KW - Legionella pneumophila

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Multiprotein Complexes

KW - Protein Binding

KW - Protein Conformation

KW - rab1 GTP-Binding Proteins

KW - Journal Article

U2 - 10.1016/j.molcel.2009.11.014

DO - 10.1016/j.molcel.2009.11.014

M3 - SCORING: Journal article

C2 - 20064470

VL - 36

SP - 1060

EP - 1072

JO - MOL CELL

JF - MOL CELL

SN - 1097-2765

IS - 6

ER -