AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling

Science

Volumn 323, Issue 5911, 2009, Pages 269-272

  Yarbrough, Melanie L ^a   Li, Yan ^b,c   Kinch, Lisa N ^d   Grishin, Nick V ^d   Ball, Haydn L ^b,c   Orth, Kim ^a  

^a UNIVERSITY OF TEXAS AT DALLAS   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^c UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^d HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE PHOSPHATE; BACTERIAL PROTEIN; PROTEIN CDC42; RAC PROTEIN; RHO FACTOR; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; THREONINE; UNCLASSIFIED DRUG; VOPS PROTEIN;

BACTERIUM; CYTOLOGY; ENZYME ACTIVITY; INHIBITION; PROTEIN; SIGNALING;

ARTICLE; CONTROLLED STUDY; CYTOSKELETON; EUKARYOTIC CELL; FEMALE; HUMAN; HUMAN CELL; MOLECULAR BIOLOGY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN PROCESSING; SIGNAL TRANSDUCTION; VIBRIO PARAHAEMOLYTICUS;

ADENOSINE MONOPHOSPHATE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CDC42 GTP-BINDING PROTEIN; CELL SHAPE; HELA CELLS; HUMANS; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; PHOSPHORYLATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; RAC GTP-BINDING PROTEINS; RECOMBINANT FUSION PROTEINS; RHO GTP-BINDING PROTEINS; SIGNAL TRANSDUCTION; THREONINE; VIBRIO PARAHAEMOLYTICUS;

EUKARYOTA; VIBRIO; VIBRIO PARAHAEMOLYTICUS;

EID: 58149400542     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1166382     Document Type: Article

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16. We thank N. Alto, R. Taussig, P. Sternweis, S. Mukherjee, M. Rosen, E. Olson, J. Goldstein, M. Brown, T. Iida, T. Honda, L. McCarter, and the Orth lab for insightful discussions, critical reading, and/or generous supply of reagents. K.O. and M.L.Y. are supported by grants from NIH-Allergy and Infectious Disease (R01-AI056404) and the Welch Foundation (I- 1561). L.N.K. and N.G. are supported by the Welch Foundation (I-1505) and Howard Hughes Medical Institute. K.O. is a Beckman Young Investigator, Burroughs Wellcome Investigator, and W. W. Caruth Biomedical Scholar.