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An Integrated System to Remotely Trigger Intracellular Signal Transduction by Upconversion Nanoparticle-mediated Kinase Photoactivation
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A pickup in pseudokinase activity.

Arvin C Dar1

  • 1Department of Oncological Sciences, Icahn School of Medicine at Mount Sinai, Tisch Cancer Institute, New York, NY 10129, USA. arvin.dar@mssm.edu

Biochemical Society Transactions
|July 19, 2013
PubMed
Summary
This summary is machine-generated.

Pseudokinases, once thought inactive, are now known to possess enzymatic activity, challenging previous assumptions about kinase function and signaling pathways. Research highlights kinase suppressor of Ras (KSR) as an active pseudokinase with allosterically regulated activity.

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Last Updated: May 9, 2026

An Integrated System to Remotely Trigger Intracellular Signal Transduction by Upconversion Nanoparticle-mediated Kinase Photoactivation
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Published on: August 30, 2017

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Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
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Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Kinases are crucial enzymes regulating cellular processes through phosphorylation.
  • Pseudokinases were historically considered inactive due to mutations in conserved active sites.
  • Emerging evidence shows some pseudokinases are enzymatically active, suggesting novel mechanisms or relaxed constraints.

Purpose of the Study:

  • To review active pseudokinases.
  • To highlight kinase suppressor of Ras (KSR) as a key example.
  • To explore allosteric regulation in pseudokinase activity.

Main Methods:

  • Literature review of biochemical and structural analyses of pseudokinases.
  • Focus on KSR (kinase suppressor of Ras) activity.
  • Analysis of allosteric mechanisms influencing kinase activity.

Main Results:

  • Several pseudokinases exhibit enzymatic activity, contrary to prior predictions.
  • KSR demonstrates regulated kinase activity, accelerated by allosteric mechanisms.
  • The kinase fold's catalytic activity or structural aspects are vital for pseudokinase function.

Conclusions:

  • Pseudokinases are not uniformly inactive and play significant roles in cellular signaling.
  • Allosteric regulation is a key mechanism for modulating pseudokinase activity, exemplified by KSR.
  • Understanding pseudokinase function requires considering their catalytic potential and structural roles.