{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Missler M"],"funding":["NIMH NIH HHS"],"pagination":["3630-8"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6793134"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(10)"],"pubmed_abstract":["Neurexophilin was discovered as a neuronal glycoprotein that is copurified with neurexin Ialpha during affinity chromatography on immobilized alpha-latrotoxin (Petrenko et al., 1996). We have now investigated how neurexophilin interacts with neurexins, whether it is post-translationally processed by site-specific cleavage similar to neuropeptides, and whether related neuropeptide-like proteins are expressed in brain. Our data show that mammalian brains contain four genes for neurexophilins the products of which share a common structure composed of five domains: an N-terminal signal peptide, a variable N-terminal domain, a highly conserved central domain that is N-glycosylated, a short linker region, and a conserved C-terminal domain that is cysteine-rich. When expressed in pheochromocytoma (PC12) cells with a replication-deficient adenovirus, neurexophilin 1 was rapidly N-glycosylated and then slowly processed to a smaller mature form, probably by endoproteolytic cleavage. Similar expression experiments in other neuron-like cells and in fibroblastic cells revealed that N-glycosylation of neurexophilin 1 occurred in all cell types tested, whereas proteolytic processing was observed only in neuron-like cells. Finally, only recombinant neurexin Ialpha and IIIalpha but not neurexin Ibeta interacted with neurexophilin 1 and were preferentially bound to the processed mature form of neurexophilin. Together our data demonstrate that neurexophilins form a family of related glycoproteins that are proteolytically processed after synthesis and bind to alpha-neurexins. The structure and characteristics of neurexophilins indicate that they function as neuropeptides that may signal via alpha-neurexins."],"journal":["The Journal of neuroscience : the official journal of the Society for Neuroscience"],"pubmed_title":["Neurexophilins form a conserved family of neuropeptide-like glycoproteins."],"pmcid":["PMC6793134"],"funding_grant_id":["R37 MH052804","MH52804"],"pubmed_authors":["Missler M","Sudhof TC"],"additional_accession":[]},"is_claimable":false,"name":"Neurexophilins form a conserved family of neuropeptide-like glycoproteins.","description":"Neurexophilin was discovered as a neuronal glycoprotein that is copurified with neurexin Ialpha during affinity chromatography on immobilized alpha-latrotoxin (Petrenko et al., 1996). We have now investigated how neurexophilin interacts with neurexins, whether it is post-translationally processed by site-specific cleavage similar to neuropeptides, and whether related neuropeptide-like proteins are expressed in brain. Our data show that mammalian brains contain four genes for neurexophilins the products of which share a common structure composed of five domains: an N-terminal signal peptide, a variable N-terminal domain, a highly conserved central domain that is N-glycosylated, a short linker region, and a conserved C-terminal domain that is cysteine-rich. When expressed in pheochromocytoma (PC12) cells with a replication-deficient adenovirus, neurexophilin 1 was rapidly N-glycosylated and then slowly processed to a smaller mature form, probably by endoproteolytic cleavage. Similar expression experiments in other neuron-like cells and in fibroblastic cells revealed that N-glycosylation of neurexophilin 1 occurred in all cell types tested, whereas proteolytic processing was observed only in neuron-like cells. Finally, only recombinant neurexin Ialpha and IIIalpha but not neurexin Ibeta interacted with neurexophilin 1 and were preferentially bound to the processed mature form of neurexophilin. Together our data demonstrate that neurexophilins form a family of related glycoproteins that are proteolytically processed after synthesis and bind to alpha-neurexins. The structure and characteristics of neurexophilins indicate that they function as neuropeptides that may signal via alpha-neurexins.","dates":{"release":"1998-01-01T00:00:00Z","publication":"1998 May","modification":"2024-11-20T05:46:33.435Z","creation":"2019-11-05T08:11:36Z"},"accession":"S-EPMC6793134","cross_references":{"pubmed":["9570794"],"doi":["10.1523/jneurosci.18-10-03630.1998","10.1523/JNEUROSCI.18-10-03630.1998"]}}