AMPylation of Rho GTPases by Vibrio VopS Disrupts Effector Binding and Downstream Signaling

被引：309

作者：

Yarbrough, Melanie L. ^{[1
]}

Li, Yan ^{[2
,3
]}

Kinch, Lisa N. ^{[4
,5
]}

Grishin, Nick V. ^{[4
,5
]}

Ball, Haydn L. ^{[2
,3
]}

Orth, Kim ^{[1
]}

机构：

[1] Univ Texas SW Med Ctr Dallas, Dept Mol Biol, Dallas, TX 75390 USA

[2] Univ Texas SW Med Ctr Dallas, Prot Chem Technol Ctr, Dallas, TX 75390 USA

[3] Univ Texas SW Med Ctr Dallas, Dept Internal Med, Dallas, TX 75390 USA

[4] Univ Texas SW Med Ctr Dallas, Howard Hughes Med Inst, Dallas, TX 75390 USA

[5] Univ Texas SW Med Ctr Dallas, Dept Biochem, Dallas, TX 75390 USA

来源：

SCIENCE | 2009年 / 323卷 / 5911期

关键词：

III SECRETION SYSTEM; PARAHAEMOLYTICUS; PROTEIN; ACTIVATION;

D O I：

10.1126/science.1166382

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The Vibrio parahaemolyticus type III effector VopS is implicated in cell rounding and the collapse of the actin cytoskeleton by inhibiting Rho guanosine triphosphatases ( GTPases). We found that VopS could act to covalently modify a conserved threonine residue on Rho, Rac, and Cdc42 with adenosine 5 '- monophosphate ( AMP). The resulting AMPylation prevented the interaction of Rho GTPases with downstream effectors, thereby inhibiting actin assembly in the infected cell. Eukaryotic proteins were also directly modified with AMP, potentially expanding the repertoire of posttranslational modifications for molecular signaling.

引用

页码：269 / 272

页数：4

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