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Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

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Quantifying phosphorylation dynamics in primary neuronal cultures using LC-MS/MS.

Kristina Desch¹, Erin M Schuman¹, Julian D Langer^1,2

¹Max Planck Institute for Brain Research, Max von Laue Strasse 4, 60438 Frankfurt, Germany.

|January 10, 2022

Summary

This summary is machine-generated.

This study details a workflow for analyzing protein phosphorylation and abundance in cultured neurons. The method uses liquid chromatography-coupled mass spectrometry for label-free quantification of proteins.

Keywords:

Cell culture Mass Spectrometry Neuroscience Protein Biochemistry Proteomics

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

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Published on: December 27, 2016

Area of Science:

Neuroscience
Cell Biology
Biochemistry

Background:

Protein phosphorylation is crucial for cellular regulation.
Controlling protein levels, location, and activity is essential for cell function.

Purpose of the Study:

To present a workflow for monitoring protein abundance and phosphorylation in primary cultured neurons.
To provide a detailed guide for the detection and label-free quantification of phosphorylated and unmodified proteins.

Main Methods:

Liquid chromatography-coupled mass spectrometry (LC-MS).
Primary cell culture of cortical neurons.
Phosphoproteomic sample preparation and data processing.

Main Results:

A comprehensive protocol for analyzing protein phosphorylation and abundance.
Label-free quantification of both phosphorylated and unmodified proteins.
Detailed steps for cell culture, sample prep, and data evaluation.

Conclusions:

The presented workflow enables robust monitoring of protein phosphorylation and abundance in neurons.
This protocol facilitates in-depth phosphoproteomic analysis of primary neuronal cultures.
The method supports the study of cellular regulation in neuroscience research.