{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Karlsson AB"],"funding":["NINDS NIH HHS","NIGMS NIH HHS"],"pagination":["1355-65"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3982999"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(8)"],"pubmed_abstract":["Troyer syndrome is an autosomal recessive hereditary spastic paraplegia (HSP) caused by frameshift mutations in the SPG20 gene that results in a lack of expression of the truncated protein. Spartin is a multifunctional protein, yet only two conserved domains--a microtubule-interacting and trafficking domain and a plant-related senescence domain involved in cytokinesis and mitochondrial physiology, respectively--have been defined. We have shown that overexpressed spartin binds to the Ile44 hydrophobic pocket of ubiquitin, suggesting spartin might contain a ubiquitin-binding domain. In the present study, we demonstrate that spartin contributes to the formation of dendritic aggresome-like induced structures (DALIS) through a unique ubiquitin-binding region (UBR). Using short hairpin RNA, we k"],"journal":["Molecular biology of the cell"],"pubmed_title":["The role of spartin and its novel ubiquitin binding region in DALIS occurrence."],"pmcid":["PMC3982999"],"funding_grant_id":["R01 GM085006","1R01NS073967-01A1","R01 NS073967"],"pubmed_authors":["Hooper C","Shekhtman A","Karlsson AB","Dimitrova V","Washington J","Bakowska JC"],"additional_accession":[]},"is_claimable":false,"name":"The role of spartin and its novel ubiquitin binding region in DALIS occurrence.","description":"Troyer syndrome is an autosomal recessive hereditary spastic paraplegia (HSP) caused by frameshift mutations in the SPG20 gene that results in a lack of expression of the truncated protein. Spartin is a multifunctional protein, yet only two conserved domains--a microtubule-interacting and trafficking domain and a plant-related senescence domain involved in cytokinesis and mitochondrial physiology, respectively--have been defined. We have shown that overexpressed spartin binds to the Ile44 hydrophobic pocket of ubiquitin, suggesting spartin might contain a ubiquitin-binding domain. In the present study, we demonstrate that spartin contributes to the formation of dendritic aggresome-like induced structures (DALIS) through a unique ubiquitin-binding region (UBR). Using short hairpin RNA, we k","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Apr","modification":"2025-04-18T17:36:13.064Z","creation":"2019-03-27T01:24:46Z"},"accession":"S-EPMC3982999","cross_references":{"pubmed":["24523286"],"doi":["10.1091/mbc.E13-11-0705"]}}