title: Proteolytic processing of tau.
abstract: Tau aggregation is a hallmark of several neurodegenerative diseases, including AD (Alzheimer's disease), although the mechanism underlying tau aggregation remains unclear. Recent studies show that the proteolysis of tau plays an important role in both tau aggregation and neurodegeneration. On one hand, truncation of tau may generate amyloidogenic tau fragments that initiate the aggregation of tau, which in turn can cause toxicity. On the other hand, truncation of tau may result in tau fragments which induce neurodegeneration through unknown mechanisms, independently of tau aggregation. Blocking the truncation of tau thus may represent a promising therapeutic approach for AD or other tauopathies. In the present paper, we summarize our data on tau cleavage in a cell model of tauopathy and major results on tau cleavage reported in the literature.
authors.affiliation: Max-Planck-Unit for Structural Molecular Biology c/o DESY, Notkestrasse 85, 22607 Hamburg, Germany.
authors.forename: Yipeng
authors.initials: Y
authors.lastname: Wang
authors.forename: Sarika
authors.initials: S
authors.lastname: Garg
authors.forename: Eva-Maria
authors.initials: EM
authors.lastname: Mandelkow
authors.forename: Eckhard
authors.initials: E
authors.lastname: Mandelkow
mesh_terms: D000818:Animals; D002478:Cells, Cultured; D011232:Chemical Precipitation; D006801:Humans; D008954:Models, Biological; D010447:Peptide Hydrolases / Q000378:metabolism*; D055503:Protein Multimerization; D011499:Protein Processing, Post-Translational / Q000502:physiology; D016875:tau Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D016875:tau Proteins; D010447:Peptide Hydrolases