{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang Y"],"funding":["NINDS NIH HHS"],"pagination":["13354-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC27228"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["97(24)"],"pubmed_abstract":["Parkinson's disease is a common neurodegenerative disorder in which familial-linked genes have provided novel insights into the pathogenesis of this disorder. Mutations in Parkin, a ring-finger-containing protein of unknown function, are implicated in the pathogenesis of autosomal recessive familial Parkinson's disease. Here, we show that Parkin binds to the E2 ubiquitin-conjugating human enzyme 8 (UbcH8) through its C-terminal ring-finger. Parkin has ubiquitin-protein ligase activity in the presence of UbcH8. Parkin also ubiquitinates itself and promotes its own degradation. We also identify and show that the synaptic vesicle-associated protein, CDCrel-1, interacts with Parkin through its ring-finger domains. Furthermore, Parkin ubiquitinates and promotes the degradation of CDCrel-1. Fami"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1."],"pmcid":["PMC27228"],"funding_grant_id":["NS38377","P50 NS038377"],"pubmed_authors":["Dawson TM","Zhang Y","Huang H","Gao J","Chung KK","Dawson VL"],"additional_accession":[]},"is_claimable":false,"name":"Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1.","description":"Parkinson's disease is a common neurodegenerative disorder in which familial-linked genes have provided novel insights into the pathogenesis of this disorder. Mutations in Parkin, a ring-finger-containing protein of unknown function, are implicated in the pathogenesis of autosomal recessive familial Parkinson's disease. Here, we show that Parkin binds to the E2 ubiquitin-conjugating human enzyme 8 (UbcH8) through its C-terminal ring-finger. Parkin has ubiquitin-protein ligase activity in the presence of UbcH8. Parkin also ubiquitinates itself and promotes its own degradation. We also identify and show that the synaptic vesicle-associated protein, CDCrel-1, interacts with Parkin through its ring-finger domains. Furthermore, Parkin ubiquitinates and promotes the degradation of CDCrel-1. Fami","dates":{"release":"2000-01-01T00:00:00Z","publication":"2000 Nov","modification":"2025-04-04T19:06:29.467Z","creation":"2019-06-06T21:33:39Z"},"accession":"S-EPMC27228","cross_references":{"pubmed":["11078524"],"doi":["10.1073/pnas.240347797"]}}