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, Jahrgang 4, Nr. 1, 01.2011, S. 72-4.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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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 -