The C-terminus of α-Synuclein Regulates its Dynamic Cellular Internalization by Neurexin 1β.

ABSTRACT: The aggregation of the disordered neuronal protein, α-Synuclein (αS), is the primary pathological feature of Parkinson's disease. Current hypotheses favor cell-to-cell spread of αS species as underlying disease progression, driving interest in identifying the molecular species and cellular processes involved in cellular internalization of αS. Prior work from our lab identified the chemically specific interaction between αS and the presynaptic adhesion protein neurexin-1β (N1β) to be capable of driving cellular internalization of both monomer and aggregated forms of αS. Here we explore the physical basis of N1β-driven internalization of αS. Specifically, we show that spontaneous internalization of αS by SH-SY5Y and HEK293 cells expressing N1β requires essentially all of the membrane-binding

SUBMITTER: Birol M 

PROVIDER: S-EPMC10848939 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature