Dataset Information

Mouse Muscle Quadricep Methylation CARM1 KO

ABSTRACT: CARM1 muscle KO mice were generated and quadricep muscle tissue was subjected to high pH strong cation exchange and immunoaffinity purification to enrich methyl peptides.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Skeletal Muscle Fiber

SUBMITTER: Nicolas Hartel

LAB HEAD: Nicholas Graham

PROVIDER: PXD028884 | Pride | 2022-08-05

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	20201129_341_KO_E2_11.raw	Raw
	20201129_342_KO_E2_16.raw	Raw
	20201129_368_WT_E2_29.raw	Raw
	20201129_369_WT_E2_14.raw	Raw
	20201129_374_KO_E2_27.raw	Raw

Items per page:

1 - 5 of 93

Publications

The CARM1 transcriptome and arginine methylproteome mediate skeletal muscle integrative biology.

vanLieshout Tiffany L TL Stouth Derek W DW Hartel Nicolas G NG Vasam Goutham G Ng Sean Y SY Webb Erin K EK Rebalka Irena A IA Mikhail Andrew I AI Graham Nicholas A NA Menzies Keir J KJ Hawke Thomas J TJ Ljubicic Vladimir V

Molecular metabolism 20220721

<h4>Objective</h4>Coactivator-associated arginine methyltransferase 1 (CARM1) catalyzes the methylation of arginine residues on target proteins to regulate critical processes in health and disease. A mechanistic understanding of the role(s) of CARM1 in skeletal muscle biology is only gradually emerging. The purpose of this study was to elucidate the function of CARM1 in regulating the maintenance and plasticity of skeletal muscle.<h4>Methods</h4>We used transcriptomic, methylproteomic, molecular ...[more]

PMID: 35872306

Similar Datasets

Project description:Protein methylation has been implicated in many important biological contexts including signaling, metabolism, and transcriptional control. Despite the importance of this post- translational modification, the global analysis of protein methylation by mass spectrometry-based proteomics has not been extensively studied due to the lack of robust, well-characterized techniques for methyl-peptidemethyl peptide enrichment. Here, to better investigate protein methylation, we optimized and compared two methods for methyl-peptidemethyl peptide enrichment: immunoaffinity purification (IAP) and high pH strong cation exchange (SCX). Comparison of these methods revealed that they are largely orthogonal for monomethyl arginine (MMA), suggesting that the usage of both techniques is required to provide a global view of protein methylation. Using both IAP and SCX, we investigated changes in protein methylation downstream of protein arginine methyltransferase 1 (PRMT1). Together, these techniques allowed us to quantify over ~1,000 arginine methylation sites on 407 proteins. Of these methylation sites, PRMT1 knockdown resulted in significant changes to 110 arginine methylation sites on 59 proteins. In contrast, zero lysine methylation sites were significantly changed upon PRMT1 knockdown. In PRMT1 knockdown cells, 24 MMA sites exhibited both significant downregulation (ie, putative PRMT1-mediated MMA targets) and 63 significant upregulation (ie, putative PRMT1-mediated ADMA targets). PRMT1 knockdown induced significant changes in asymmetric dimethyl arginine (ADMA), consistent with being PRMT1 targets. Additionally, We also observed that PRMT1 knockdown induced significant increases in symmetric dimethyl arginine (SDMA) methylation, suggesting that loss of PRMT1 activity allows scavenging of PRMT1 substrates by Type II PRMTs. Analysis of the subcellular localization and protein function of the significantly changing methyl-proteins revealed that the majority of PRMT1 substrates are localized to the nucleus and involved in RNA and DNA binding. Taken together, our results suggest that deep protein methylation profiling by mass spectrometry requires orthogonal enrichment techniques, identify novel PRMT1 methylation targets, and highlight in order to understand the dynamic interplay between methyltransferases in mammalian cells.