TY - JOUR
T1 - The elusive activity of the Yersinia protein kinase A kinase domain is revealed
AU - Laskowski-Arce, Michelle A.
AU - Orth, Kim
N1 - Funding Information:
We thank the members of the K.O. laboratory for helpful discussions and critical reading of the manuscript. This work was funded in part by NIH-NIAID (M.L.-A.) (R01-AI056404 and R21-DK072134) and the Welch Research Foundation (I-1561). K.O. is a W.W. Caruth Jr. Scholar in Biomedical Research and a Burrougjs Wellcome Investigator in Pathogenesis of Infectious Disease.
PY - 2007/10
Y1 - 2007/10
N2 - 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 Gαq, and inhibits Gαq-mediated signaling. Inhibition by YpkA could contribute to one of the most documented symptoms of Yersinia pestis infection, extensive bleeding.
AB - 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 Gαq, and inhibits Gαq-mediated signaling. Inhibition by YpkA could contribute to one of the most documented symptoms of Yersinia pestis infection, extensive bleeding.
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U2 - 10.1016/j.tim.2007.09.002
DO - 10.1016/j.tim.2007.09.002
M3 - Short survey
C2 - 17920275
AN - SCOPUS:35649004349
SN - 0966-842X
VL - 15
SP - 437
EP - 440
JO - Trends in Microbiology
JF - Trends in Microbiology
IS - 10
ER -