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

Desch, Kristina; Schuman, Erin M.; Langer, Julian David

doi:10.1016/j.xpro.2021.101063

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

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Langer, Julian David
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Desch, K., Schuman, E. M., & Langer, J. D. (2022). Quantifying phosphorylation dynamics in primary neuronal cultures using LC-MS/MS. STAR Protocols, 3(1): 101063. doi:10.1016/j.xpro.2021.101063.

Cite as: https://hdl.handle.net/21.11116/0000-0009-C28E-C

Abstract

Cellular processes require tight and coordinated control of protein abundance, localization, and activity. One of the core mechanisms to achieve specific regulation of proteins is protein phosphorylation. Here we present a workflow to monitor protein abundance and phosphorylation in primary cultured neurons using liquid chromatography-coupled mass spectrometry. Our protocol provides a detailed guide on all steps for detection and label-free-quantification of phosphorylated and unmodified proteins of primary cortical neurons, including primary cell culture, phosphoproteomic sample preparation and data-processing, and evaluation