Article
A conserved arginine within the αC-helix of Erk1/2 is a latch of autoactivation and of oncogenic capabilities.
The Journal of biological chemistry - 1 Sept 2023
Soudah Nadine, Baskin Alexey, Smorodinsky-Atias Karin, Beenstock Jonah, Ganon Yifat, Hayouka Ruchama, Aboraya Mohammed, Livnah Oded, Ilouz Ronit, Engelberg David
Abstract excerpt
Eukaryotic protein kinases (EPKs) adopt an active conformation following phosphorylation of a particular activation loop residue. Most EPKs spontaneously autophosphorylate this residue. While structure-function relationships of the active conformation are essentially understood, those of the "prone-to-autophosphorylate" conformation are unclear. Here, we propose that a site within the αC-helix of EPKs, occupied...
Topics
- Phosphorylation
- Arginine
- Humans
- Animals
- Mice
- Cell Line
- HEK293 Cells
- Enzyme Activation
- Mutation
- Saccharomyces cerevisiae
- Mitogen-Activated Protein Kinase 1