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Updated: Jan 28, 2026

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

Myc and its interactors take shape.

William B Tu¹, Sara Helander², Robert Pilstål²

¹Department of Medical Biophysics, Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada; Princess Margaret Cancer Centre, University Health Network, Toronto, Ontario, Canada.

Biochimica Et Biophysica Acta

|June 17, 2014

Summary

This summary is machine-generated.

The Myc oncoprotein drives cancer by regulating gene expression. Understanding its structure and protein interactions, like with Max, is crucial for cancer research and developing new therapies.

Keywords:

Cancer Myc Post-translational modification Protein structure Protein–protein interaction Transcriptional regulation

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Area of Science:

Molecular Biology
Oncology
Structural Biology

Background:

The Myc oncoprotein is a significant factor in human cancer development.
Myc is a global regulator of gene expression, with its function extensively studied for over 30 years.

Purpose of the Study:

To review key insights into Myc interactors and protein structure.
To understand Myc's roles in transcriptional regulation and cancer.

Main Methods:

Review of genome-wide studies and structural analyses of Myc.
Examination of Myc's protein-protein interactions and its interactome.

Main Results:

Structural analyses reveal transient regions in Myc mediating interactions and functions.
Key interactors like Max, TRRAP, and PTEF-b offer mechanistic insights into transcriptional activity.
Ubiquitin ligases regulate Myc protein stability.

Conclusions:

Myc's large interactome requires further functional elucidation.
Future research should utilize advanced genome-wide and proteome-wide approaches to understand Myc's mechanisms.
This review contributes to understanding Myc proteins in cell biology and pathology.