Modulation of small GTPases by Legionella
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Modulation of small GTPases by Legionella. / Goody, Roger S; Itzen, Aymelt.
In: CURR TOP MICROBIOL, Vol. 376, 2013, p. 117-33.Research output: SCORING: Contribution to journal › SCORING: Review article › Research
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TY - JOUR
T1 - Modulation of small GTPases by Legionella
AU - Goody, Roger S
AU - Itzen, Aymelt
PY - 2013
Y1 - 2013
N2 - The pathogenic bacterium Legionella pneumophila interacts intimately with signaling molecules during the infection of eukaryotic host cells. Among a diverse set of regulatory molecules, host small GTPases appear to be prominent and significant targets. Small GTPases are molecular switches that regulate cellular signaling via their respective nucleotide-bound states: When bound to GDP, they are inactive, but become activated upon binding to GTP. Legionella secretes specific bacterial proteins into the cytosol of the host cell that most prominently modulate the activities of small GTPases involved in vesicular trafficking, but probably also other G-proteins. The master regulators of vesicular trafficking, i.e., Rab and Arf proteins, are majorly targeted G-proteins of Legionella proteins, and among these, Rab1 experiences the most diverse modifications. Generally, the activities of small GTPases are modulated by GDP/GTP exchange (activation), GTP hydrolysis (deactivation), membrane recruitment, post-translational modifications (phosphocholination, adenylylation), and tight and competitive binding. Here, we discuss the consequences and molecular details of the modulation of small GTPases for the infection by Legionella, with a special but not exclusive focus on Rab and Arf proteins.
AB - The pathogenic bacterium Legionella pneumophila interacts intimately with signaling molecules during the infection of eukaryotic host cells. Among a diverse set of regulatory molecules, host small GTPases appear to be prominent and significant targets. Small GTPases are molecular switches that regulate cellular signaling via their respective nucleotide-bound states: When bound to GDP, they are inactive, but become activated upon binding to GTP. Legionella secretes specific bacterial proteins into the cytosol of the host cell that most prominently modulate the activities of small GTPases involved in vesicular trafficking, but probably also other G-proteins. The master regulators of vesicular trafficking, i.e., Rab and Arf proteins, are majorly targeted G-proteins of Legionella proteins, and among these, Rab1 experiences the most diverse modifications. Generally, the activities of small GTPases are modulated by GDP/GTP exchange (activation), GTP hydrolysis (deactivation), membrane recruitment, post-translational modifications (phosphocholination, adenylylation), and tight and competitive binding. Here, we discuss the consequences and molecular details of the modulation of small GTPases for the infection by Legionella, with a special but not exclusive focus on Rab and Arf proteins.
KW - ADP-Ribosylation Factor 1
KW - Humans
KW - Legionella
KW - Monomeric GTP-Binding Proteins
KW - rab1 GTP-Binding Proteins
KW - Journal Article
KW - Review
U2 - 10.1007/82_2013_340
DO - 10.1007/82_2013_340
M3 - SCORING: Review article
C2 - 23918171
VL - 376
SP - 117
EP - 133
JO - CURR TOP MICROBIOL
JF - CURR TOP MICROBIOL
SN - 0070-217X
ER -