{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7(12)"],"submitter":["Tsai YC"],"pubmed_abstract":["Synphilin-1 has been identified as an interaction partner of α-synuclein, a key protein in the pathogenesis of Parkinson disease (PD). To further explore novel binding partners of synphilin-1, a yeast two hybrid screening was performed and kalirin-7 was identified as a novel interactor. We then investigated the effect of kalirin-7 on synphilin-1 aggregate formation. Coexpression of kalirin-7 and synphilin-1 caused a dramatic relocation of synphilin-1 cytoplasmic small inclusions to a single prominent, perinuclear inclusion. These perinuclear inclusions were characterized as being aggresomes according to their colocalization with microtubule organization center markers, and their formation was microtubule-dependent. Furthermore, kalirin-7 increased the susceptibility of synphilin-1 inclusio"],"journal":["PloS one"],"pagination":["e51999"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3527391"],"repository":["biostudies-literature"],"pubmed_title":["The Guanine nucleotide exchange factor kalirin-7 is a novel synphilin-1 interacting protein and modifies synphilin-1 aggregate transport and formation."],"pmcid":["PMC3527391"],"pubmed_authors":["Soehn AS","Nguyen HP","Tsai YC","Riess O"],"additional_accession":[]},"is_claimable":false,"name":"The Guanine nucleotide exchange factor kalirin-7 is a novel synphilin-1 interacting protein and modifies synphilin-1 aggregate transport and formation.","description":"Synphilin-1 has been identified as an interaction partner of α-synuclein, a key protein in the pathogenesis of Parkinson disease (PD). To further explore novel binding partners of synphilin-1, a yeast two hybrid screening was performed and kalirin-7 was identified as a novel interactor. We then investigated the effect of kalirin-7 on synphilin-1 aggregate formation. Coexpression of kalirin-7 and synphilin-1 caused a dramatic relocation of synphilin-1 cytoplasmic small inclusions to a single prominent, perinuclear inclusion. These perinuclear inclusions were characterized as being aggresomes according to their colocalization with microtubule organization center markers, and their formation was microtubule-dependent. Furthermore, kalirin-7 increased the susceptibility of synphilin-1 inclusio","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012","modification":"2025-05-31T23:34:00.891Z","creation":"2025-05-31T23:34:00.891Z"},"accession":"S-EPMC3527391","cross_references":{"pubmed":["23284848"],"doi":["10.1371/journal.pone.0051999"]}}