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Structural requirements for Yersinia YopJ inhibition of MAP kinase pathways.


ABSTRACT: MAPK signaling cascades are evolutionally conserved. The bacterial effector, YopJ, uses the unique activity of Ser/Thr acetylation to inhibit the activation of the MAPK kinase (MKK) and prevent activation by phosphorylation. YopJ is also able to block yeast MAPK signaling pathways using this mechanism. Based on these observations, we performed a genetic screen to isolate mutants in the yeast MKK, Pbs2, that suppress YopJ inhibition. One suppressor contains a mutation in a conserved tyrosine residue and bypasses YopJ inhibition by increasing the basal activity of Pbs2. Mutations on the hydrophobic face of the conserved G alpha-helix in the kinase domain prevent both binding and acetylation by YopJ. Corresponding mutants in human MKKs showed that they are conserved not only structurally, but also functionally. These studies reveal a conserved binding site found on the superfamily of MAPK kinases while providing insight into the molecular interactions required for YopJ inhibition.

SUBMITTER: Hao YH 

PROVIDER: S-EPMC2147050 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature

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Structural requirements for Yersinia YopJ inhibition of MAP kinase pathways.

Hao Yi-Heng YH   Wang Yong Y   Burdette Dara D   Mukherjee Sohini S   Keitany Gladys G   Goldsmith Elizabeth E   Orth Kim K  

PloS one 20080102 1


MAPK signaling cascades are evolutionally conserved. The bacterial effector, YopJ, uses the unique activity of Ser/Thr acetylation to inhibit the activation of the MAPK kinase (MKK) and prevent activation by phosphorylation. YopJ is also able to block yeast MAPK signaling pathways using this mechanism. Based on these observations, we performed a genetic screen to isolate mutants in the yeast MKK, Pbs2, that suppress YopJ inhibition. One suppressor contains a mutation in a conserved tyrosine resi  ...[more]

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