CHIP-mediated hyperubiquitylation of tau promotes its self-assembly into the insoluble tau filaments
Ji Hyeon Kim, Jeeyoung Lee, Won Hoon Choi, Seoyoung Park, Seo Hyeong Park, Jung Hoon Lee, Sang Min Lim, Ji Young Mun, Hyun‐Soo Cho, Dohyun Han, Young Ho Suh, Min Jae Lee
Abstract
and delayed its aggregation in cultured cells including primary cultured neurons. Our biochemical findings point to a "multiple-hit model," where sequential events of tau phosphorylation and hyperubiquitylation function as a key driver of the fibrillization process, thus indicating that targeting tau ubiquitylation may be an effective strategy to alleviate the course of tauopathies.
Topics & Concepts
TauopathyTau proteinUbiquitinCrosstalkIn vitroChemistryPhosphorylationCell biologyBiophysicsBiochemistryBiologyNeurodegenerationAlzheimer's diseaseGeneDiseaseMedicinePathologyPhysicsOpticsAlzheimer's disease research and treatmentsCellular transport and secretionEndoplasmic Reticulum Stress and Disease