Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

Dimerization in protein kinase signaling.

Steven Pelech¹

¹The Brain Research Centre, Division of Neurology, 2211 Wesbrook Mall, University of British Columbia, Vancouver, BC V6T 2B5, Canada. spelech@kinexus.ca

Journal of Biology

|August 2, 2006

Summary

Mitogen-activated protein kinases ERK1 and ERK2 have opposing roles in Ras-mediated cell proliferation. Kinase dimerization may explain these findings and regulate protein phosphorylation.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

A phosphorylated variant of the mast/stem cell growth factor receptor KIT is upregulated in dorsal root ganglia of Friedreich ataxia.

Histology and histopathology·2026

Same author

Glycogen synthase kinase 3 inhibition controls <i>Mycobacterium tuberculosis</i> infection.

iScience·2024

Same author

Phosphoproteome Microarray Analysis of Extracellular Particles as a Tool to Explore Novel Biomarker Candidates for Alzheimer's Disease.

International journal of molecular sciences·2024

Same author

Lipid- and phospho-regulation of CTP:Phosphocholine Cytidylyltransferase α association with nuclear lipid droplets.

Molecular biology of the cell·2024

Same author

CAT PETR: a graphical user interface for differential analysis of phosphorylation and expression data.

Statistical applications in genetics and molecular biology·2023

Same author

Characterization of Developmentally Regulated cAMP/Ca

Development, growth & differentiation·2023

Area of Science:

Cellular Biology
Molecular Biology
Biochemistry

Background:

Mitogen-activated protein kinases (MAPKs), specifically ERK1 and ERK2, are crucial regulators of cell proliferation.
Ras-mediated signaling pathways are fundamental to cellular growth and differentiation.
Opposing roles for closely related kinases present a regulatory puzzle.

Purpose of the Study:

To investigate the underlying mechanism for the opposing roles of ERK1 and ERK2 in Ras-mediated cell proliferation.
To propose a novel regulatory paradigm involving kinase dimerization.

Main Methods:

The study likely involved in vitro kinase assays and cell-based assays to examine ERK1 and ERK2 activity and interactions.
Analysis of Ras-mediated signaling pathways and their impact on cell proliferation.

Main Results:

ERK1 and ERK2 exhibit opposing functions in Ras-driven cell proliferation.
Evidence suggests that dimerization of ERK1 and ERK2 could be responsible for their distinct roles.

Conclusions:

Kinase dimerization is proposed as a mechanism explaining the opposing roles of ERK1 and ERK2.
This dimerization-dependent regulation may represent a common paradigm for controlling protein phosphorylation events.

Related Experiment Videos