The MAPK kinase Pek1 acts as a phosphorylation-dependent molecular switch

Article Abstract:

It has been possible to identify Pek1, a specific mitogen-activated protein kinase (MAPK) kinase (MAPKK) for Pmk1 MAPK. In its unphosphorylated form, Pek1 acts as a strong negative regulator of Pmk1 MAPK signalling. Unphosphorylated Pek1 binds phosphorylated Pmk1 and inhibits its kinase activity, thus attenuating the signalling. This is the first time that it has been shown that a MAPK-activating kinase is also a negative regulator of the same MAPK.

Protein kinases, Mitogens

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A new group of conserved coactivators that increase the specificity of AP-1 transcription factors

Article Abstract:

The Jun proteins are characterized by near-identical sequence-recognition characteristics. A new, previously unreported Jun protein that interacts with c-Jun and JunD, but not with JunB or v-Jun, was investigated. Designated JAB-1, the new protein selectively potentiates transactivation by only c-Jun or JunD. JAB-1 does not have any effect on the binding of either JunB or v-Jun and it stabilizes complexes of c-Jun or JunD with AP-1 sites.

Genetic transcription, Transcription (Genetics), Ribosomal proteins

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Feedback regulation of MAPK signaling by an RNA-binding protein

Article Abstract:

Research shows that an RNA-binding protein in yeast, Rnc1 functions as a negative regulator of Pmk1 signaling, indicating that Rnc1 is a component of a negative-feedback loop involved in the regulation of the Pmk1 pathway via its binding to Pmp1 mRNA. These results suggest that mitogen-activated protein kinase (MAPK) mediated signaling is under negative-feedback control through MAPK phosphatase expression.

Japan, Analysis, Physiological aspects, Cellular signal transduction, Enzyme regulation, Biofeedback training, Biofeedback, Binding proteins

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