Journal
SCIENCE
Volume 312, Issue 5777, Pages 1211-1214Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1126867
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Funding
- NIAID NIH HHS [R01-AI056404] Funding Source: Medline
- NIDDK NIH HHS [R21-DK072134] Funding Source: Medline
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Yersinia species use a variety of type III effector proteins to target eukaryotic signaling systems. The effector Yop) inhibits mitogen-activated protein kinase (MAPK) and the nu clear factor kappa B (NF kappa B) signaling pathways used in innate immune response by preventing activation of the family of MAPK kinases (MAPKK). We show that Yop) 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.
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