Journal
MOLECULAR CELL
Volume 26, Issue 4, Pages 465-477Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2007.04.025
Keywords
-
Categories
Ask authors/readers for more resources
Pathogenic bacteria of the genus Yersinia employ a type III secretion system to inject bacterial effector proteins directly into the host cytosol. One of these effectors, the Yersinia serine/ threonine protein kinase YpkA, is an essential virulence determinant involved in host actin cytoskeletal rearrangements and in inhibition of phagocytosis. Here we report that YpkA inhibits multiple G alpha q signaling pathways. The kinase activity of YpkA is required for G alpha q inhibition. YpkA phosphorylates Ser47, a key residue located in the highly conserved diphosphate binding loop of the GTPase fold of G alpha q. YpkA-mediated phosphorylation of Ser47 impairs guanine nucleotide binding by G alpha q. Y. pseudotuberculosis expressing wild-type YpkA, but not a catalytically inactive YpkA mutant, interferes with G alpha q-mediated signaling pathways. Identification of a YpkA-mediated phosphorylation site in G alpha q sheds light on the contribution of the kinase activity of YpkA to Yersinia pathogenesis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available