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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
Published on: April 29, 2022
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Controlling Ser/Thr protein phosphatase PP1 activity and function through interaction with regulatory subunits
Antonio Casamayor1, Joaquín Ariño1
1Institut de Biotecnologia i Biomedicina & Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Cerdanyola, del Vallès, Spain.
Advances in Protein Chemistry and Structural Biology
|September 21, 2020
Summary
Protein phosphatase 1 (PP1C) is a key enzyme in cells, regulated by various subunits. These regulatory proteins control PP1C
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Protein phosphatase 1 (PP1C) is a major serine/threonine phosphatase in eukaryotic cells.
- PP1C comprises a catalytic subunit with broad substrate specificity.
- PP1C activity is modulated by a vast array of regulatory subunits, forming diverse holoenzymes.
Purpose of the Study:
- To introduce the catalytic subunit of Protein Phosphatase 1 (PP1C).
- To review the principal families of PP1C regulatory subunits.
- To emphasize the structural basis of PP1C regulatory subunit interactions.
Main Methods:
- Literature review of PP1C regulatory subunits.
- Analysis of structural data for PP1C-regulatory subunit complexes.
- Functional characterization of PP1C holoenzymes.
Main Results:
- PP1C's catalytic subunit (PP1C) interacts with numerous regulatory proteins.
- These interactions generate holoenzymes with diverse cellular functions.
- Many regulatory subunits inhibit PP1C activity, modulating its function.
Conclusions:
- The diversity of PP1C holoenzymes underlies its extensive cellular roles.
- Understanding the structural basis of subunit interaction is crucial for deciphering PP1C regulation.
- Regulatory subunits play a critical role in fine-tuning PP1C activity and function.
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