<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7(12)</volume><submitter>Tsai YC</submitter><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</pubmed_abstract><journal>PloS one</journal><pagination>e51999</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3527391</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>The Guanine nucleotide exchange factor kalirin-7 is a novel synphilin-1 interacting protein and modifies synphilin-1 aggregate transport and formation.</pubmed_title><pmcid>PMC3527391</pmcid><pubmed_authors>Soehn AS</pubmed_authors><pubmed_authors>Nguyen HP</pubmed_authors><pubmed_authors>Tsai YC</pubmed_authors><pubmed_authors>Riess O</pubmed_authors></additional><is_claimable>false</is_claimable><name>The Guanine nucleotide exchange factor kalirin-7 is a novel synphilin-1 interacting protein and modifies synphilin-1 aggregate transport and formation.</name><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</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012</publication><modification>2025-05-31T23:34:00.891Z</modification><creation>2025-05-31T23:34:00.891Z</creation></dates><accession>S-EPMC3527391</accession><cross_references><pubmed>23284848</pubmed><doi>10.1371/journal.pone.0051999</doi></cross_references></HashMap>