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Pathogenic bacteria use the type III secretion system to delivereffector proteins into host cells to modulate the host signalingpathways. In this study, the Shigella type III effector OspFwas shown to inactivate mitogen-activated protein kinases (MAPKs)[extracellular signal–regulated kinases 1 and 2 (Erk1/2),c-Jun N-terminal kinase, and p38]. OspF irreversibly removedphosphate groups from the phosphothreonine but not from thephosphotyrosine residue in the activation loop of MAPKs. Massspectrometry revealed a mass loss of 98 daltons in p-Erk2, dueto the abstraction of the proton concomitant with cleavageof the C-OP bond in the phosphothreonine residue. This unexpectedenzymatic activity, termed phosphothreonine lyase, appearedspecific for MAPKs and was shared by other OspF family members.
National Institute of Biological Sciences, Beijing, 102206, China.
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: shaofeng{at}nibs.ac.cn
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proton concomitant with cleavage of the C-OP bond in the phosphothreonine residue. This unexpected enzymatic activity, termed phosphothreonine lyase, appeared specific for MAPKs and was shared by other OspF family members. 
To whom correspondence should be addressed. E-mail: 
