<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>44(2)</volume><submitter>Steiman S</submitter><funding>Faculty of Science, York University</funding><funding>Canadian Institutes of Health Research</funding><pubmed_abstract>Myocyte enhancer factor 2 (MEF2) proteins are involved in multiple developmental, physiological, and pathological processes in vertebrates. Protein-protein interactions underlie the plethora of biological processes impacted by MEF2A, necessitating a detailed characterization of the MEF2A interactome. A nanobody based affinity-purification/mass spectrometry strategy was employed to achieve this goal. Specifically, the MEF2A protein complexes were captured from myogenic lysates using a GFP-tagged MEF2A protein immobilized with a GBP-nanobody followed by LC-MS/MS proteomic analysis to identify MEF2A interactors. After bioinformatic analysis, we further characterized the interaction of MEF2A with a transcriptional repressor, FOXP1. FOXP1 coprecipitated with MEF2A in proliferating myogenic cell</pubmed_abstract><journal>Molecular and cellular biology</journal><pagination>57-71</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10950271</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>FoxP1 Represses MEF2A in Striated Muscle.</pubmed_title><pmcid>PMC10950271</pmcid><pubmed_authors>Steiman S</pubmed_authors><pubmed_authors>McDermott JC</pubmed_authors><pubmed_authors>Miyake T</pubmed_authors></additional><is_claimable>false</is_claimable><name>FoxP1 Represses MEF2A in Striated Muscle.</name><description>Myocyte enhancer factor 2 (MEF2) proteins are involved in multiple developmental, physiological, and pathological processes in vertebrates. Protein-protein interactions underlie the plethora of biological processes impacted by MEF2A, necessitating a detailed characterization of the MEF2A interactome. A nanobody based affinity-purification/mass spectrometry strategy was employed to achieve this goal. Specifically, the MEF2A protein complexes were captured from myogenic lysates using a GFP-tagged MEF2A protein immobilized with a GBP-nanobody followed by LC-MS/MS proteomic analysis to identify MEF2A interactors. After bioinformatic analysis, we further characterized the interaction of MEF2A with a transcriptional repressor, FOXP1. FOXP1 coprecipitated with MEF2A in proliferating myogenic cell</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024</publication><modification>2026-04-08T18:30:12.28Z</modification><creation>2025-04-04T20:26:00.995Z</creation></dates><accession>S-EPMC10950271</accession><cross_references><pubmed>38483114</pubmed><doi>10.1080/10985549.2024.2323959</doi></cross_references></HashMap>