{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["44(2)"],"submitter":["Steiman S"],"funding":["Faculty of Science, York University","Canadian Institutes of Health Research"],"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"],"journal":["Molecular and cellular biology"],"pagination":["57-71"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10950271"],"repository":["biostudies-literature"],"pubmed_title":["FoxP1 Represses MEF2A in Striated Muscle."],"pmcid":["PMC10950271"],"pubmed_authors":["Steiman S","McDermott JC","Miyake T"],"additional_accession":[]},"is_claimable":false,"name":"FoxP1 Represses MEF2A in Striated Muscle.","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","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024","modification":"2026-04-08T18:30:12.28Z","creation":"2025-04-04T20:26:00.995Z"},"accession":"S-EPMC10950271","cross_references":{"pubmed":["38483114"],"doi":["10.1080/10985549.2024.2323959"]}}