{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Platsaki S"],"funding":["European Research Council"],"pagination":["16267-16279"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7705314"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["295(48)"],"pubmed_abstract":["Punctin/MADD-4, a member of the ADAMTSL extracellular matrix protein family, was identified as an anterograde synaptic organizer in the nematode <i>Caenorhabditis elegans.</i> At GABAergic neuromuscular junctions, the short isoform MADD-4B binds the ectodomain of neuroligin NLG-1, itself a postsynaptic organizer of inhibitory synapses. To identify the molecular bases of their partnership, we generated recombinant forms of the two proteins and carried out a comprehensive biochemical and biophysical study of their interaction, complemented by an <i>in vivo</i> localization study. We show that spontaneous proteolysis of MADD-4B first generates a shorter N-MADD-4B form, which comprises four thrombospondin (TSP) domains and one Ig-like domain and binds NLG-1. A second processing event eliminate"],"journal":["The Journal of biological chemistry"],"pubmed_title":["The Ig-like domain of Punctin/MADD-4 is the primary determinant for interaction with the ectodomain of neuroligin NLG-1."],"pmcid":["PMC7705314"],"funding_grant_id":["695295"],"pubmed_authors":["Platsaki S","Marchot P","Delauzun V","Bourne Y","Bessereau JL","Zhou X","Pinan-Lucarre B","Fourquet P","Tu H","Mansuelle P"],"additional_accession":[]},"is_claimable":false,"name":"The Ig-like domain of Punctin/MADD-4 is the primary determinant for interaction with the ectodomain of neuroligin NLG-1.","description":"Punctin/MADD-4, a member of the ADAMTSL extracellular matrix protein family, was identified as an anterograde synaptic organizer in the nematode <i>Caenorhabditis elegans.</i> At GABAergic neuromuscular junctions, the short isoform MADD-4B binds the ectodomain of neuroligin NLG-1, itself a postsynaptic organizer of inhibitory synapses. To identify the molecular bases of their partnership, we generated recombinant forms of the two proteins and carried out a comprehensive biochemical and biophysical study of their interaction, complemented by an <i>in vivo</i> localization study. We show that spontaneous proteolysis of MADD-4B first generates a shorter N-MADD-4B form, which comprises four thrombospondin (TSP) domains and one Ig-like domain and binds NLG-1. A second processing event eliminate","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Nov","modification":"2026-04-29T09:09:48.128Z","creation":"2022-02-11T13:12:29.421Z"},"accession":"S-EPMC7705314","cross_references":{"pubmed":["32928959"],"doi":["10.1074/jbc.ra120.014591","10.1074/jbc.RA120.014591"]}}