Kinesin light chain-1 isoform E does not interact with calsyntenin-1. Issue 18 (16th December 2015)

• Record Type: Journal Article
• Authors: Uchida, Yoko; Gomi, Fujiya
• Is Part Of: NeuroReport. Volume 26:Issue 18(2015)
• Publication Date: 2015-12-16
• Subjects: calsyntenin-1 -- kinesin light chain-1 isoform E -- protein–protein interactions; Neurosciences -- Periodicals; Nervous system -- Periodicals; Neurophysiology -- Periodicals; Nervous System Diseases -- Periodicals; Nervous System Physiological Phenomena -- Periodicals; Neurosciences -- Periodicals; 616.805
• DOI: 10.1097/WNR.0000000000000486
• Languages: English
• ISSNs: 0959-4965

Abstract

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. Abstract : Supplemental Digital Content is available in the text.