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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.
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Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Related Experiment Video

Updated: Mar 24, 2026

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Published on: April 20, 2018

SplitTurboID mapping of dimeric protein phosphatase complex interactomes.

Abishankari Rajkumar¹, Antoine Gaudreau-Lapierre¹, Curtis L F Anthony¹

¹Department of Cellular and Molecular Medicine and Ottawa Institute of Systems Biology, Faculty of Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada.

|March 23, 2026

Summary

This summary is machine-generated.

Protein phosphatase 1 (PP1) promiscuity is resolved using splitTurboID to map specific catalytic-regulatory subunit interactions. This method precisely identifies PP1 complex localization and substrate specificity, advancing our understanding of cellular signaling pathways.

Keywords:

Biochemical research method Biochemistry Biological sciences

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Last Updated: Mar 24, 2026

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

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

Published on: April 29, 2022

Area of Science:

Molecular Biology
Biochemistry
Cell Biology

Background:

Protein Phosphatase 1 (PP1) is a key enzyme in cellular regulation.
PP1's function is dictated by its association with numerous regulatory subunits, influencing its localization and substrate specificity.
Existing methods for mapping PP1 interactions lack conditional analysis of specific holoenzyme complexes.

Purpose of the Study:

To develop and validate a novel proximity interactome mapping technique for distinct catalytic-regulatory subunit pairs of PP1.
To achieve high spatial resolution and conditional analysis of PP1 holoenzyme complexes.
To demonstrate the general applicability of the method for studying other protein-protein interactions.

Main Methods:

Adaptation of a splitTurboID fragment complementation assay.
Proximal interactome mapping of specific PP1 catalytic-regulatory subunit pairs.
Development of an analysis pipeline to identify unique and enriched interactors, distinguishing them from common contaminants.

Main Results:

The splitTurboID approach reliably maps the proximal interactome of PP1 holoenzymes with high spatial resolution.
The analysis pipeline effectively identifies specific interacting partners and filters out contaminants.
A newly identified regulatory subunit's associations with both PP1 and other proteins were confirmed.

Conclusions:

SplitTurboID is a powerful and versatile tool for dissecting the composition and function of specific protein complexes, such as PP1 holoenzymes.
This technique provides crucial insights into the conditional regulation of enzyme activity and localization.
The method's general applicability extends to the study of diverse protein-protein interactions beyond PP1 complexes.