Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation

Sohini Mukherjee, Gladys Keitany, Yan Li, Yong Wang, Haydn L. Ball, Elizabeth J. Goldsmith, Kim Orth

Research output: Contribution to journalArticle

411 Scopus citations

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 phosphorylation, preventing activation of the modified protein. This covalent modification may be used as a general regulatory mechanism in biological signaling.

Original languageEnglish (US)
Pages (from-to)1211-1214
Number of pages4
JournalScience
Volume312
Issue number5777
DOIs
StatePublished - May 26 2006

ASJC Scopus subject areas

  • General

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