{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Luebbers A"],"funding":["NINDS NIH HHS","Israel National Road Safety Authority","National Institutes of Health","Texas A&M University Health Science Center","NIH HHS"],"pagination":["47-59.e7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10872408"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(1)"],"pubmed_abstract":["It is well established that G-protein-coupled receptors (GPCRs) stimulated by neurotransmitters are critical for neuromodulation. Much less is known about how heterotrimeric G-protein (Gαβγ) regulation after receptor-mediated activation contributes to neuromodulation. Recent evidence indicates that the neuronal protein GINIP shapes GPCR inhibitory neuromodulation via a unique mechanism of G-protein regulation that controls pain and seizure susceptibility. However, the molecular basis of this mechanism remains ill-defined because the structural determinants of GINIP responsible for binding and regulating G proteins are not known. Here, we combined hydrogen-deuterium exchange mass spectrometry, computational structure predictions, biochemistry, and cell-based biophysical assays to demonstrat"],"journal":["Structure (London, England : 1993)"],"pubmed_title":["Dissecting the molecular basis for the modulation of neurotransmitter GPCR signaling by GINIP."],"pmcid":["PMC10872408"],"funding_grant_id":["R01 NS117101","F31NS115318","R01NS117101","SCR_019063","F31 NS115318"],"pubmed_authors":["Zhou M","Gonzalez-Hernandez AJ","Eyles SJ","Levitz J","Luebbers A","Garcia-Marcos M"],"additional_accession":[]},"is_claimable":false,"name":"Dissecting the molecular basis for the modulation of neurotransmitter GPCR signaling by GINIP.","description":"It is well established that G-protein-coupled receptors (GPCRs) stimulated by neurotransmitters are critical for neuromodulation. Much less is known about how heterotrimeric G-protein (Gαβγ) regulation after receptor-mediated activation contributes to neuromodulation. Recent evidence indicates that the neuronal protein GINIP shapes GPCR inhibitory neuromodulation via a unique mechanism of G-protein regulation that controls pain and seizure susceptibility. However, the molecular basis of this mechanism remains ill-defined because the structural determinants of GINIP responsible for binding and regulating G proteins are not known. Here, we combined hydrogen-deuterium exchange mass spectrometry, computational structure predictions, biochemistry, and cell-based biophysical assays to demonstrat","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jan","modification":"2025-04-04T12:02:36.859Z","creation":"2025-04-04T12:02:36.859Z"},"accession":"S-EPMC10872408","cross_references":{"pubmed":["37989308"],"doi":["10.1016/j.str.2023.10.010"]}}