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Proteomics

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
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Updated: May 27, 2026

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

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Published on: April 29, 2022

Mapping Phosphorylation-Specific Pin1-CRMP2 Interactions Using an Integrated Mass Spectrometry Approach.

Danielle F Kay¹, Nikolas J Brooks¹, Simon G Caulton¹

¹School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.

ACS Chemical Biology

|May 26, 2026

Summary

This summary is machine-generated.

Pin1 interacts with Collapsin Response Mediator Protein-2 (CRMP2), a key protein in Alzheimer's Disease pathogenesis. This interaction, dependent on CRMP2 phosphorylation, suggests Pin1 may regulate neurofibrillary tangle formation.

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Abnormal protein phosphorylation drives Alzheimer's Disease (AD) pathogenesis, forming neurofibrillary tangles.
Pin1, a cis-trans prolyl isomerase, is implicated in AD progression and regulates phosphoprotein function.

Purpose of the Study:

To investigate the molecular interaction between Pin1 and Collapsin Response Mediator Protein-2 (CRMP2).
To elucidate the role of Pin1 in modulating CRMP2 phosphorylation in the context of Alzheimer's Disease.

Main Methods:

Native mass spectrometry to identify Pin1-CRMP2 binding.
Hydrogen-deuterium exchange mass spectrometry to map the binding interface.
Analysis of CRMP2 phosphorylation sites (Thr509, Thr514) and their impact on binding affinity.

Main Results:

A novel interaction interface between Pin1 and the C-terminus of CRMP2 was identified.
Pin1 binding to CRMP2 is phosphorylation-dependent, with specific residues enhancing affinity.
The WW domain of Pin1 was localized as the binding site for CRMP2.

Conclusions:

Pin1 binds to hyperphosphorylated CRMP2, a component of neurofibrillary tangles.
These findings suggest a regulatory mechanism for Pin1 in modulating CRMP2 hyperphosphorylation.
This interaction offers new insights into the molecular pathways of Alzheimer's Disease.