What question did this study set out to answer?

The study aims to identify a protein kinase that regulates c-Jun activation through phosphorylation in response to specific stimuli.

November 1, 1993Genes & DevelopmentOpen Access

Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.

View Full Paper

Ask AI

Bookmark

The study aims to identify a protein kinase that regulates c-Jun activation through phosphorylation in response to specific stimuli.
Identified a serine/threonine kinase activated by oncogenes and UV light.
Analyzed the binding of this kinase to the c-Jun trans-activation domain.
Investigated the effects of mutations on kinase binding and c-Jun response.
The identified kinase, termed JNK, potently phosphorylates c-Jun at serines 63 and 73, enhancing its activity.
Binding of JNK to c-Jun leads to the dissociation of their complex upon phosphorylation.
Mutations affecting the kinase-binding site reduced c-Jun’s response to Ha-Ras and UV.

Discussion

No takes yet. Share an insight, caveat, or question.

Implication

Randomized trial identifies a kinase that enhances c-Jun activity through phosphorylation in response to oncogenes and UV light, highlighting regulatory mechanisms.

Cite This Study

Hibi et al. (1993) studied this question.

synapsesocial.com/papers/6a0cd8663b13d695db1f55ec https://doi.org/10.1101/gad.7.11.2135

View Full Paper

Ask AI

Bookmark

Implication

Randomized trial identifies a kinase that enhances c-Jun activity through phosphorylation in response to oncogenes and UV light, highlighting regulatory mechanisms.

Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.

Key Points

Discussion

Implication

Cite This Study

Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.

Key Points

Discussion

Implication

Cite This Study

Also Consider

Also Consider