Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation

被引:481
作者
Mukherjee, Sohini
Keitany, Gladys
Li, Yan
Wang, Yong
Ball, Haydn L.
Goldsmith, Elizabeth J.
Orth, Kim [1 ]
机构
[1] Univ Texas, SW Med Ctr, Dept Mol Biol, Dallas, TX 75390 USA
[2] Univ Texas, SW Med Ctr, Prot Chem Technol Ctr, Dallas, TX 75390 USA
[3] Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75390 USA
关键词
D O I
10.1126/science.1126867
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
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页码:1211 / 1214
页数:4
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