The regulation of protein function by multisite phosphorylation--a 25 year update

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Updated: Oct 10, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

P Cohen1

  • 1MRC Protein Phosphorylation Unit, MSI/WTB Complex, University of Dundee, Dundee, UK DD1 5EH. pcohen@dundee.ac.uk

Trends in Biochemical Sciences
|December 16, 2000
PubMed

Insights

Protein phosphorylation, a key regulatory process, significantly alters protein behavior and function. Multisite phosphorylation integrates cellular signals, controlling response extent and duration.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Protein phosphorylation is a crucial post-translational modification regulating diverse cellular processes.
  • The functional outcomes of phosphorylation include changes in protein activity, localization, stability, and interactions.

Purpose of the Study:

  • To elucidate the multifaceted roles of protein phosphorylation in cellular regulation.
  • To highlight the significance of multisite phosphorylation in signal integration and response dynamics.

Main Methods:

  • Literature review and synthesis of existing research on protein phosphorylation.
  • Analysis of case studies demonstrating the impact of multisite phosphorylation.

Main Results:

  • Phosphorylation modulates protein intrinsic activity, subcellular localization, and half-life.
  • Multisite phosphorylation allows for combinatorial effects on protein function.
  • Multisite phosphorylation is essential for integrating multiple signals and fine-tuning cellular responses.

Conclusions:

  • Protein phosphorylation is a versatile regulatory mechanism with broad functional consequences.
  • Multisite phosphorylation provides a sophisticated platform for signal integration, enhancing cellular responsiveness and adaptability.

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