Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation.

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Mukherjee S, Keitany G, Li Y, Wang Y, Ball HL, Goldsmith EJ, Orth K

Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation.

Science. 2006 May 26;312(5777):1211-4.

PubMed ID
16728640 [ View in PubMed
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Abstract

Yersinia species use a variety of type III effector proteins to target eukaryotic signaling systems. The effector YopJ inhibits mitogen-activated protein kinase (MAPK) and the nuclear factor kappaB (NFkappaB) signaling pathways used in innate immune response by preventing activation of the family of MAPK kinases (MAPKK). We show that YopJ acted as an acetyltransferase, using acetyl-coenzyme A (CoA) to modify the critical serine and threonine residues in the activation loop of MAPKK6 and thereby blocking phosphorylation. The acetylation on MAPKK6 directly competed with phosphorylation, preventing activation of the modified protein. This covalent modification may be used as a general regulatory mechanism in biological signaling.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Dual specificity mitogen-activated protein kinase kinase 1Q02750Details
Inhibitor of nuclear factor kappa-B kinase subunit betaO14920Details
Dual specificity mitogen-activated protein kinase kinase 3P46734Details
Dual specificity mitogen-activated protein kinase kinase 5Q13163Details
Dual specificity mitogen-activated protein kinase kinase 6P52564Details