Associated Papers
All intrinsically active Erk1/2 mutants autophosphorylate threonine207/188, a plausible regulator of the TEY motif phosphorylation.
Baskin A et al.
The Journal of Biological Chemistry, 2025
A conserved arginine within the αC-helix of Erk1/2 is a latch of autoactivation and of oncogenic capabilities.
Soudah N et al.
The Journal of Biological Chemistry, 2023
TRIM15 and CYLD regulate ERK activation via lysine-63-linked polyubiquitination.
Zhu G et al.
Nature Cell Biology, 2021
Mutations That Confer Drug-Resistance, Oncogenicity and Intrinsic Activity on the ERK MAP Kinases-Current State of the Art.
Smorodinsky-Atias K et al.
Cells, 2020
An Activating Mutation in ERK Causes Hyperplastic Tumors in a scribble Mutant Tissue in Drosophila.
Kushnir T et al.
Genetics, 2020
Monoubiquitination of p120-catenin is essential for TGFβ-induced epithelial-mesenchymal transition and tumor metastasis.
Wu Q et al.
Science Advances, 2020
Variants of the yeast MAPK Mpk1 are fully functional independently of activation loop phosphorylation.
Goshen-Lago T et al.
Molecular Biology of the Cell, 2016
Intrinsically active variants of Erk oncogenically transform cells and disclose unexpected autophosphorylation capability that is independent of TEY phosphorylation.
Smorodinsky-Atias K et al.
Molecular Biology of the Cell, 2016
Isolation of intrinsically active (MEK-independent) variants of the ERK family of mitogen-activated protein (MAP) kinases.
Levin-Salomon V et al.
The Journal of Biological Chemistry, 2008
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