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Published Online November 27, 2008
Science DOI: 10.1126/science.1166382

Reports

Submitted on September 25, 2008
Accepted on November 14, 2008

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

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

1 Department of Molecular Biology, UT Southwestern Medical Center, Dallas, TX 75390, USA.
2 Protein Chemistry Technology Center, UT Southwestern Medical Center, Dallas, TX 75390, USA.; Department of Internal Medicine, UT Southwestern Medical Center, Dallas, TX 75390, USA.
3 HHMI; Department of Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390, USA.

* To whom correspondence should be addressed.
Kim Orth , E-mail: Kim.Orth{at}utsouthwestern.edu

The Vibrio parahaemolyticus type III effector VopS is implicated in cell rounding and the collapse of the actin cytoskeleton by inhibiting Rho GTPases. We found that VopS could act as an AMPylator to covalently modify a conserved threonine residue on Rho, Rac, and Cdc42 with adenosine 5’-monophosphate. The resulting AMPylation prevented 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.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)