BibTex format
@article{Young:2014:10.1038/ncomms6887,
author = {Young, JC and Clements, A and Lang, AE and Garnett, JA and Munera, D and Arbeloa, A and Pearson, J and Hartland, EL and Matthews, SJ and Mousnier, A and Barry, DJ and Way, M and Schlosser, A and Aktories, K and Frankel, G},
doi = {10.1038/ncomms6887},
journal = {Nature Communications},
title = {The Escherichia coli effector EspJ blocks Src kinase activity via amidation and ADP ribosylation},
url = {http://dx.doi.org/10.1038/ncomms6887},
volume = {5},
year = {2014}
}
RIS format (EndNote, RefMan)
TY - JOUR
AB - The hallmark of enteropathogenic Escherichia coli (EPEC) infection is the formation of actin-rich pedestal-like structures, which are generated following phosphorylation of the bacterial effector Tir by cellular Src and Abl family tyrosine kinases. This leads to recruitment of the Nck–WIP–N-WASP complex that triggers Arp2/3-dependent actin polymerization in the host cell. The same phosphorylation-mediated signalling network is also assembled downstream of the Vaccinia virus protein A36 and the phagocytic Fc-gamma receptor FcγRIIa. Here we report that the EPEC type-III secretion system effector EspJ inhibits autophosphorylation of Src and phosphorylation of the Src substrates Tir and FcγRIIa. Consistent with this, EspJ inhibits actin polymerization downstream of EPEC, Vaccinia virus and opsonized red blood cells. We identify EspJ as a unique adenosine diphosphate (ADP) ribosyltransferase that directly inhibits Src kinase by simultaneous amidation and ADP ribosylation of the conserved kinase-domain residue, Src E310, resulting in glutamine-ADP ribose.
AU - Young,JC
AU - Clements,A
AU - Lang,AE
AU - Garnett,JA
AU - Munera,D
AU - Arbeloa,A
AU - Pearson,J
AU - Hartland,EL
AU - Matthews,SJ
AU - Mousnier,A
AU - Barry,DJ
AU - Way,M
AU - Schlosser,A
AU - Aktories,K
AU - Frankel,G
DO - 10.1038/ncomms6887
PY - 2014///
SN - 2041-1723
TI - The Escherichia coli effector EspJ blocks Src kinase activity via amidation and ADP ribosylation
T2 - Nature Communications
UR - http://dx.doi.org/10.1038/ncomms6887
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000347686600001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - http://hdl.handle.net/10044/1/21445
VL - 5
ER -
