Yersinia inhibits host signaling by acetylating MAPK kinases.

Abstract:

:Pathogenic Yersinia spp. secrete the effector YopJ (YopP) into host cells to counteract cytokine production and to induce programmed cell death (apoptosis). YopJ achieves these aims by inactivating mitogen-activated protein kinase (MAPK) and nuclear factor kappaB signaling pathways. YopJ was shown to bind to members of the MAPK kinase (MKK) family and was predicted to have protease activity toward ubiquitin (Ub)-like proteins. In a recent report, YopJ was demonstrated to inactivate MKKs via acetylation of critical serine or threonine residues. The ramifications of these exciting results are discussed in the context of other studies implicating YopJ as a Ub-like protease.

journal_name

ACS Chem Biol

journal_title

ACS chemical biology

authors

Bliska JB

doi

10.1021/cb600261k

subject

Has Abstract

pub_date

2006-07-21 00:00:00

pages

349-51

issue

6

eissn

1554-8929

issn

1554-8937

journal_volume

1

pub_type

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