Mapping Cellular Protein Lysine Methylation Using Targeted-Mass Spectrometry.

Anand Chopra, Matthew Hoekstra, William G Willmore, Kyle K Biggar

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Anand ChopraThe Shraga Segal Department of Microbiology, Immunology and Genetics, Ben-Gurion University of the Negev, Be'er-Sheva, Israel.

Matthew HoekstraInstitute of Biochemistry, Carleton University, Ottawa, ON, Canada.

William G WillmoreInstitute of Biochemistry, Carleton University, Ottawa, ON, Canada. bill.willmore@carleton.ca.

Kyle K BiggarInstitute of Biochemistry, Carleton University, Ottawa, ON, Canada. kyle.biggar@carleton.ca.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine methylation is a dynamic posttranslation modification (PTM) involved in the regulation of numerous biological processes. Depending on the context, site- and state-specific lysine methylation has been shown to regulate key features of proteins, such as stability, activity, and interactions. Assessing site- and state-specific lysine methylation within the proteome is difficult without access to antibodies that are able to detect the modification site. As the commercially available options for reliable antibodies that are specific to a methylation site and state are limited, mass spectrometry (MS)-based methods are more appealing as they enable detection of site- and state-specific methylation events with broad applicability. Here, we describe the use of immunoprecipitation and targeted-MS to detect and perform relative quantification of site-specific lysine methylation events occurring on endogenous proteins of interest. As an example, detection and relative quantification of hypoxia-responsive PGC1α-K224me2 and RNF20-K610me3/K614me3 lysine methylation, occurring in hypoxia-treated human colorectal cancer cells, are described.

Indexed as

LysineMass SpectrometryProtein Processing, Post-TranslationalProteomicsHumansImmunoprecipitationMethylationLysineHypoxiaLysine methylationParallel reaction monitoringPosttranslational modificationTargeted-mass spectrometry

Identifiers

PMID42542527

DOI10.1016/j.molcel.2019.09.019

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.