Research ExplorerPublicationsThe versatile Legionella effector protein DrrA

The versatile Legionella effector protein DrrA

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The versatile Legionella effector protein DrrA. / Goody, Roger S; Schoebel, Stefan; Oesterlin, Lena K; Blümer, Julia; Peters, Heide; Blankenfeldt, Wulf; Itzen, Aymelt.

In: Commun Integr Biol, Vol. 4, No. 1, 01.2011, p. 72-4.

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

Harvard

Goody, RS, Schoebel, S, Oesterlin, LK, Blümer, J, Peters, H, Blankenfeldt, W & Itzen, A 2011, 'The versatile Legionella effector protein DrrA', Commun Integr Biol, vol. 4, no. 1, pp. 72-4. https://doi.org/10.4161/cib.4.1.13857

APA

Goody, R. S., Schoebel, S., Oesterlin, L. K., Blümer, J., Peters, H., Blankenfeldt, W., & Itzen, A. (2011). The versatile Legionella effector protein DrrA. Commun Integr Biol, 4(1), 72-4. https://doi.org/10.4161/cib.4.1.13857

Vancouver

Goody RS, Schoebel S, Oesterlin LK, Blümer J, Peters H, Blankenfeldt W et al. The versatile Legionella effector protein DrrA. Commun Integr Biol. 2011 Jan;4(1):72-4. https://doi.org/10.4161/cib.4.1.13857

Bibtex

@article{ef35060867ba4c8fb9f7bbec27725763,
title = "The versatile Legionella effector protein DrrA",
abstract = "The human pathogen Legionella pneumophila is a bacterium that infects human cells and interferes with intracellular signaling. The Legionella protein DrrA is one of the numerous effectors that the bacterium translocates into the host cytosol. DrrA binds to the Legionella containing vacuole (LCV), an organelle in which Legionella survives and replicates, and recruits and activates the vesicular trafficking regulator Rab1 to redirect vesicular trafficking between the endoplasmatic reticulum and the Golgi. After depositing Rab1 at the LCV, DrrA covalently modifies Rab1 with an AMP moiety at a specific tyrosine residue (Tyr77), which is centrally located in the functionally important switch II region. This adenylylation reaction interferes with the deactivation of Rab1 by GTPase activating proteins (GAPs), thereby presumably prolonging the active state of the protein at the LCV. Here, we summarize the versatile properties of DrrA and speculate on the effects of Rab1-adenylylation.",
keywords = "Journal Article",
author = "Goody, {Roger S} and Stefan Schoebel and Oesterlin, {Lena K} and Julia Bl{\"u}mer and Heide Peters and Wulf Blankenfeldt and Aymelt Itzen",
year = "2011",
month = jan,
doi = "10.4161/cib.4.1.13857",
language = "English",
volume = "4",
pages = "72--4",
number = "1",

}

RIS

TY - JOUR

T1 - The versatile Legionella effector protein DrrA

AU - Goody, Roger S

AU - Schoebel, Stefan

AU - Oesterlin, Lena K

AU - Blümer, Julia

AU - Peters, Heide

AU - Blankenfeldt, Wulf

AU - Itzen, Aymelt

PY - 2011/1

Y1 - 2011/1

N2 - The human pathogen Legionella pneumophila is a bacterium that infects human cells and interferes with intracellular signaling. The Legionella protein DrrA is one of the numerous effectors that the bacterium translocates into the host cytosol. DrrA binds to the Legionella containing vacuole (LCV), an organelle in which Legionella survives and replicates, and recruits and activates the vesicular trafficking regulator Rab1 to redirect vesicular trafficking between the endoplasmatic reticulum and the Golgi. After depositing Rab1 at the LCV, DrrA covalently modifies Rab1 with an AMP moiety at a specific tyrosine residue (Tyr77), which is centrally located in the functionally important switch II region. This adenylylation reaction interferes with the deactivation of Rab1 by GTPase activating proteins (GAPs), thereby presumably prolonging the active state of the protein at the LCV. Here, we summarize the versatile properties of DrrA and speculate on the effects of Rab1-adenylylation.

AB - The human pathogen Legionella pneumophila is a bacterium that infects human cells and interferes with intracellular signaling. The Legionella protein DrrA is one of the numerous effectors that the bacterium translocates into the host cytosol. DrrA binds to the Legionella containing vacuole (LCV), an organelle in which Legionella survives and replicates, and recruits and activates the vesicular trafficking regulator Rab1 to redirect vesicular trafficking between the endoplasmatic reticulum and the Golgi. After depositing Rab1 at the LCV, DrrA covalently modifies Rab1 with an AMP moiety at a specific tyrosine residue (Tyr77), which is centrally located in the functionally important switch II region. This adenylylation reaction interferes with the deactivation of Rab1 by GTPase activating proteins (GAPs), thereby presumably prolonging the active state of the protein at the LCV. Here, we summarize the versatile properties of DrrA and speculate on the effects of Rab1-adenylylation.

KW - Journal Article

U2 - 10.4161/cib.4.1.13857

DO - 10.4161/cib.4.1.13857

M3 - SCORING: Journal article

C2 - 21509184

VL - 4

SP - 72

EP - 74

IS - 1

ER -