title: Kinesin light chain-1 isoform E does not interact with calsyntenin-1.
abstract: β-Amyloid is generated by the sequential cleavage of amyloid precursor protein. Calsyntenin-1 and kinesin light chain-1 splice variant E (KLC1-E) have been proposed to regulate β-amyloid production from amyloid precursor protein. Vesicles containing calsyntenin-1 are transported from the Golgi apparatus to axons by interaction between calsyntenin-1 and KLC1 in their C-terminal regions. However, it is unclear whether KLC1 isoform E influences the interaction between KLC1 and calsyntenin-1, resulting in the impaired axonal transport of calsyntenin-1 vesicles. Here, we show that KLC1-E does not interact with calsyntenin-1 using a pull-down assay, coimmunoprecipitation, and immunocytochemistry. These findings suggest that KLC1-E enrichment may impair the axonal transport of calsyntenin-1 vesicles.
authors.affiliation: Research Team for Aging Neuroscience, Tokyo Metropolitan Institute of Gerontology, Tokyo, Japan.
authors.forename: Yoko
authors.initials: Y
authors.lastname: Uchida
authors.forename: Fujiya
authors.initials: F
authors.lastname: Gomi
mesh_terms: D000818:Animals; D019556:COS Cells; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D002522:Chlorocebus aethiops; D016547:Kinesins; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D051189:Murinae; D020033:Protein Isoforms / Q000378:metabolism
chemical_list: D002135:Calcium-Binding Proteins; D008869:Microtubule-Associated Proteins; D020033:Protein Isoforms; D016547:Kinesins