The elusive activity of the Yersinia protein kinase A kinase domain is revealed.
Yersinia spp. pathogens use their type III secretion system to translocate effectors that manipulate host signaling pathways during infection. Although molecular targets for five of the six known Yersinia effectors are known, the target for the serine/threonine kinase domain of Yersinia protein kinase A (YpkA) has remained elusive. Recently, Navarro et al. (2007) demonstrated that YpkA phosphorylates Galphaq, and inhibits Galphaq-mediated signaling. Inhibition by YpkA could contribute to one of the most documented symptoms of Yersinia pestis infection, extensive bleeding.
Laskowski-Arce
Michelle A
MA
Department of Molecular Biology, UT Southwestern Medical Center, 6000 Harry Hines Blvd, Dallas, TX 75390-9148, USA.
Orth
Kim
K
D000818:Animals; D002217:Carbachol / Q000494:pharmacology; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry / Q000378:metabolism*; D043802:GTP-Binding Protein alpha Subunits, Gq-G11 / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D043562:Receptors, G-Protein-Coupled / Q000187:drug effects / Q000378:metabolism*; D015398:Signal Transduction; D015007:Yersinia / Q000201:enzymology* / Q000472:pathogenicity; D015009:Yersinia Infections / Q000382:microbiology* / Q000503:physiopathology
D043562:Receptors, G-Protein-Coupled; D002217:Carbachol; D017868:Cyclic AMP-Dependent Protein Kinases; D043802:GTP-Binding Protein alpha Subunits, Gq-G11