{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sticco MJ"],"funding":["NCATS NIH HHS","Swiss National Science Foundation","NIDA NIH HHS","Charles H. Hood Foundation","National Institutes of Health","National Institute on Drug Abuse","NIH HHS","Max-Planck-Gesellschaft"],"pagination":["e21194"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11565477"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["35(1)"],"pubmed_abstract":["Synapses are the fundamental structural unit by which neurons communicate. An orchestra of proteins regulates diverse synaptic functions, including synapse formation, maintenance, and elimination-synapse homeostasis. Some proteins of the larger C1q super-family are synaptic organizers involved in crucial neuronal processes in various brain regions. C1Q-like (C1QL) proteins bind to the adhesion G protein-coupled receptor B3 (ADGRB3) and act at synapses in a subset of circuits. To investigate the hypothesis that the secreted C1QL proteins mediate tripartite trans-synaptic adhesion complexes, we conducted an in vivo interactome study and identified new binding candidates. We demonstrate that C1QL3 mediates a novel cell-cell adhesion complex involving ADGRB3 and two neuronal pentraxins, NPTX1 and NPTXR. Analysis of single-cell RNA-Seq data from the cerebral cortex shows that C1ql3, Nptx1, and Nptxr are highly co-expressed in the same excitatory neurons. Thus, our results suggest the possibility that in vivo the three co-expressed proteins are presynaptically secreted and form a complex capable of binding to postsynaptically localized ADGRB3, thereby creating a novel trans-synaptic adhesion complex. Identifying new binding partners for C1QL proteins and deciphering their underlying molecular principles will accelerate our understanding of their role in synapse organization."],"journal":["FASEB journal : official publication of the Federation of American Societies for Experimental Biology"],"pubmed_title":["C1QL3 promotes cell-cell adhesion by mediating complex formation between ADGRB3/BAI3 and neuronal pentraxins."],"pmcid":["PMC11565477"],"funding_grant_id":["F32 DA031654","166815","CRETP3_166815","#UL1TR001108","UL1 TR001108"],"pubmed_authors":["Thompson BL","Foldy C","Pena Palomino PA","Lukacsovich D","Sticco MJ","Martinelli DC","Ressl S"],"additional_accession":[]},"is_claimable":false,"name":"C1QL3 promotes cell-cell adhesion by mediating complex formation between ADGRB3/BAI3 and neuronal pentraxins.","description":"Synapses are the fundamental structural unit by which neurons communicate. An orchestra of proteins regulates diverse synaptic functions, including synapse formation, maintenance, and elimination-synapse homeostasis. Some proteins of the larger C1q super-family are synaptic organizers involved in crucial neuronal processes in various brain regions. C1Q-like (C1QL) proteins bind to the adhesion G protein-coupled receptor B3 (ADGRB3) and act at synapses in a subset of circuits. To investigate the hypothesis that the secreted C1QL proteins mediate tripartite trans-synaptic adhesion complexes, we conducted an in vivo interactome study and identified new binding candidates. We demonstrate that C1QL3 mediates a novel cell-cell adhesion complex involving ADGRB3 and two neuronal pentraxins, NPTX1 and NPTXR. Analysis of single-cell RNA-Seq data from the cerebral cortex shows that C1ql3, Nptx1, and Nptxr are highly co-expressed in the same excitatory neurons. Thus, our results suggest the possibility that in vivo the three co-expressed proteins are presynaptically secreted and form a complex capable of binding to postsynaptically localized ADGRB3, thereby creating a novel trans-synaptic adhesion complex. Identifying new binding partners for C1QL proteins and deciphering their underlying molecular principles will accelerate our understanding of their role in synapse organization.","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jan","modification":"2026-06-02T03:35:02.952Z","creation":"2025-04-04T12:01:02.059Z"},"accession":"S-EPMC11565477","cross_references":{"pubmed":["33337553"],"doi":["10.1096/fj.202000351RR","10.1096/fj.202000351rr"]}}