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Originally published in Science Express on 27 November 2008
Science 9 January 2009:
Vol. 323. no. 5911, pp. 269 - 272
DOI: 10.1126/science.1166382
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Reports

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

Melanie L. Yarbrough,1 Yan Li,2,3 Lisa N. Kinch,4 Nick V. Grishin,4 Haydn L. Ball,2,3 Kim Orth1*

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.

1 Department of Molecular Biology, University of Texas (UT) Southwestern Medical Center, Dallas, TX 75390, USA.
2 Protein Chemistry Technology Center, UT Southwestern Medical Center, Dallas, TX 75390, USA.
3 Department of Internal Medicine, UT Southwestern Medical Center, Dallas, TX 75390, USA.
4 Howard Hughes Medical Institute and Department of Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390, USA.

* To whom correspondence should be addressed. E-mail: kim.orth{at}utsouthwestern.edu

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