1. Yersinia YopJ Acetylates and Inhibits Kinase Activation by Blocking Phosphorylation.
- Author
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Mukherjee, Sohini, Keitany, Gladys, Yan Li, Yong Wang, Ball, Haydn L., Goldsmith, Elizabeth J., and Orth, Kim
- Subjects
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YERSINIA , *IMMUNE response , *CHEMICAL reactions , *MITOGEN-activated protein kinases , *ACETYLCOENZYME A , *PHOSPHOTRANSFERASES , *ACYLATION , *AMINO acids , *ACETYLTRANSFERASES - 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 κB (NFκB) 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 acetylcoenzyme 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 phosphorytation, preventing activation of the modified protein. This covalent modification may be used as a general regulatory mechanism in biological signaling. [ABSTRACT FROM AUTHOR]
- Published
- 2006
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