{"id":18549,"date":"2024-02-02T15:21:07","date_gmt":"2024-02-02T20:21:07","guid":{"rendered":"https:\/\/www.bumc.bu.edu\/biochemcellbio\/?p=18549"},"modified":"2026-01-07T15:12:32","modified_gmt":"2026-01-07T20:12:32","slug":"new-publication-sheds-light-onto-the-molecular-basis-of-neurotransmitter-signaling","status":"publish","type":"post","link":"https:\/\/www.bumc.bu.edu\/biochemcellbio\/2024\/02\/02\/new-publication-sheds-light-onto-the-molecular-basis-of-neurotransmitter-signaling\/","title":{"rendered":"New publication sheds light onto the molecular basis of neurotransmitter signaling"},"content":{"rendered":"

A new paper led by Alex Luebbers in the Garcia-Marcos Lab dissects the molecular basis for how GINIP, a G\u03b1i-interacting protein in neurons involved in controlling pain and seizures, modulates GPCR responses triggered by neurotransmitters. GINIP mimics how G-protein signaling effectors bind to G\u03b1 subunits via its PHD domain to differentially scale discrete G-protein signaling branches. The paper has been published in Structure (https:\/\/www.sciencedirect.com\/science\/article\/abs\/pii\/S0969212623003891?via%3Dihub<\/a>), and was previously posted on bioRxiv (https:\/\/www.biorxiv.org\/content\/10.1101\/2023.04.20.537566v1<\/a>).\"\"<\/p>\n

This paper builds and explands on another paper recently published in the same lab establishing that the neuronal protein GINIP shapes GPCR inhibitory neuromodulation via a unique mechanism of G-protein regulation that controls pain and seizure susceptibility (Park, Luebbers, et al Molecular Cell, 2023). However, the molecular basis of this mechanism remained ill-defined because the structural determinants of GINIP responsible for binding and regulating G proteins were not known. The newly published paper combined hydrogen-deuterium exchange mass spectrometry, computational structure predictions, biochemistry, and cell-based biophysical assays to demonstrate an effector-like binding mode of GINIP to G\u03b1i. These findings explain the molecular basis for a post-receptor mechanism of G-protein regulation that fine-tunes inhibitory neuromodulation.<\/p>\n

This paper features collaborations with the labs of Stephen Eyles at UMass-Amherst and of Joshua Levitz at Weill Cornell.<\/p>\n","protected":false},"excerpt":{"rendered":"

A new paper led by Alex Luebbers in the Garcia-Marcos Lab dissects the molecular basis for how GINIP, a G\u03b1i-interacting […]<\/p>\n","protected":false},"author":8106,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":[],"categories":[104,4654,1],"tags":[],"_links":{"self":[{"href":"https:\/\/www.bumc.bu.edu\/biochemcellbio\/wp-json\/wp\/v2\/posts\/18549"}],"collection":[{"href":"https:\/\/www.bumc.bu.edu\/biochemcellbio\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.bumc.bu.edu\/biochemcellbio\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/biochemcellbio\/wp-json\/wp\/v2\/users\/8106"}],"replies":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/biochemcellbio\/wp-json\/wp\/v2\/comments?post=18549"}],"version-history":[{"count":2,"href":"https:\/\/www.bumc.bu.edu\/biochemcellbio\/wp-json\/wp\/v2\/posts\/18549\/revisions"}],"predecessor-version":[{"id":18553,"href":"https:\/\/www.bumc.bu.edu\/biochemcellbio\/wp-json\/wp\/v2\/posts\/18549\/revisions\/18553"}],"wp:attachment":[{"href":"https:\/\/www.bumc.bu.edu\/biochemcellbio\/wp-json\/wp\/v2\/media?parent=18549"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/biochemcellbio\/wp-json\/wp\/v2\/categories?post=18549"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/biochemcellbio\/wp-json\/wp\/v2\/tags?post=18549"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}