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Updated: Jun 3, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

Kinase condensates enrich ATP and trigger autophosphorylation.

Nicholas E Lea¹, Lindsay B Case¹

¹Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.

|June 1, 2026

Summary

This summary is machine-generated.

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Kinase phase separation concentrates kinases and ATP, enhancing autophosphorylation and activating signaling pathways. This mechanism boosts kinase activity by forming signaling condensates.

Area of Science:

Biochemistry
Cell Biology
Molecular Biology

Background:

Kinase signaling regulates cellular processes via autophosphorylation.
Kinase phase separation into condensates is a known phenomenon.
The impact of condensates on kinase autophosphorylation remains unclear.

Purpose of the Study:

To investigate how kinase phase separation affects autophosphorylation.
To determine the role of condensates in kinase activation.
To explore the chemical environment within kinase condensates.

Main Methods:

Biochemical reconstitution experiments.
Cellular studies.
Analysis of kinase and ATP concentrations within condensates.

Keywords:

ABL CP: Cell biology CP: Molecular biology FAK MST autophosphorylation condensates kinase phase separation signaling

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Main Results:

Phase separation concentrates kinases (FAK, Abl, Mst2), triggering trans-autophosphorylation.
Kinase condensates enrich ATP concentration.
Positively charged intrinsically disordered regions contribute to ATP enrichment.

Conclusions:

Kinase phase separation is a general mechanism for kinase activation.
Condensates enhance signaling by concentrating both kinases and ATP.
This process locally triggers autophosphorylation and activates signaling pathways.