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

Related Concept Videos

Inhibition of Cdk Activity

Inhibition of Cdk Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...

Inhibition of CDK Activity

Inhibition of CDK Activity

PI3K/mTOR/AKT Signaling Pathway

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a...

The JAK-STAT Signaling Pathway

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...

Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

You might also read

Related Articles

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

Sort by

Same author

Preservation of Human Colonic Stem Cells Requires an ERK Dynamics Checkpoint Mediated by AKT.

bioRxiv : the preprint server for biology·2026

Same author

Wnt signaling is modulated by the buffer-like properties of cadherins.

Molecular biology of the cell·2026

Same author

Coordination of nuclear RNA processing by speckle-localized kinase TAOK2.

bioRxiv : the preprint server for biology·2025

Same author

Kinase interaction analysis predicts actions of the WNK-OSR1/SPAK pathway.

Communications biology·2025

Same author

SMURF1/2 Are Novel Regulators of WNK1 Stability.

Kinases and phosphatases·2025

Same author

Activation of WNK1 signaling through Piezo1.

Proceedings of the National Academy of Sciences of the United States of America·2025

Same journal

Vascular RhoJ Is an Effective and Selective Target for Tumor Angiogenesis and Vascular Disruption.

Cancer cell·2026

Same journal

Intratumoral B cells under stress.

Cancer cell·2026

Same journal

Chronic stress unleashes an intratumor phage-fibroblast-B cell circuit to promote tumor growth.

Cancer cell·2026

Same journal

Molecular phenotypes and spatial archetypes: A new framework for cancer-associated fibroblasts.

Cancer cell·2026

Same journal

OpenIO: An open framework for AI-native immunotherapy.

Cancer cell·2026

Same journal

From prediction to interpretation in computational pathology.

Cancer cell·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Apr 5, 2026

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Published on: October 23, 2019

A Kinase Divided.

Aroon S Karra¹, Clinton A Taylor¹, Curtis A Thorne¹

¹Department of Pharmacology, UT Southwestern Medical Center, Dallas, TX 75390, USA.

|August 13, 2015

Summary

This summary is machine-generated.

Researchers discovered a small molecule that stops ERK protein dimerization, offering a new way to fight drug-resistant cancers by targeting protein interactions instead of just enzyme activity.

More Related Videos

Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries

Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries

Published on: January 22, 2019

A Method for Screening and Validation of Resistant Mutations Against Kinase Inhibitors

A Method for Screening and Validation of Resistant Mutations Against Kinase Inhibitors

Published on: December 7, 2014

Related Experiment Videos

Last Updated: Apr 5, 2026

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Published on: October 23, 2019

Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries

Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries

Published on: January 22, 2019

A Method for Screening and Validation of Resistant Mutations Against Kinase Inhibitors

A Method for Screening and Validation of Resistant Mutations Against Kinase Inhibitors

Published on: December 7, 2014

Area of Science:

Oncology
Molecular Biology
Drug Discovery

Background:

Kinase signaling pathways, such as the ERK pathway, are crucial in cancer development and progression.
Drug resistance remains a significant challenge in cancer therapy, often linked to aberrant kinase signaling.
Targeting protein-protein interactions is an emerging strategy in drug development.

Purpose of the Study:

To identify novel therapeutic strategies for overcoming drug resistance in cancer.
To investigate the role of ERK dimerization in cancer signaling.
To evaluate a small molecule inhibitor targeting ERK dimerization.

Main Methods:

Utilized biochemical assays to assess the effect of a small molecule on ERK dimerization.
Investigated the molecule's impact on ERK catalytic activity and MEK-mediated phosphorylation.
Evaluated the anti-tumorigenic potential of the identified small molecule.

Main Results:

Identified a novel small molecule with anti-tumorigenic properties.
The small molecule specifically inhibits ERK dimerization without affecting its catalytic activity.
Demonstrated that MEK-mediated phosphorylation of ERK is independent of ERK dimerization.

Conclusions:

Targeting protein dimerization, specifically ERK dimerization, is a viable therapeutic strategy.
Inhibiting kinase signaling through protein-protein interaction blockade offers a promising approach to combat drug resistance.
This study opens new avenues for developing targeted cancer therapies.