Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation
- PMID: 16728640
- DOI: 10.1126/science.1126867
Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation
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.
Comment in
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Microbiology. Bacteria seize control by acetylating host proteins.Science. 2006 May 26;312(5777):1150-1. doi: 10.1126/science.1128785. Science. 2006. PMID: 16731519 No abstract available.
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