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000153283 1001_ $$0P:(DE-2719)9000315$$aUkmar-Godec, Tina$$b0$$eFirst author
000153283 245__ $$aProteasomal degradation of the intrinsically disordered protein tau at single-residue resolution
000153283 260__ $$aWashington, DC [u.a.]$$bAssoc.$$c2020
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000153283 520__ $$aIntrinsically disordered proteins (IDPs) can be degraded in a ubiquitin-independent process by the 20S proteasome. Decline in 20S activity characterizes neurodegenerative diseases. Here, we examine 20S degradation of IDP tau, a protein that aggregates into insoluble deposits in Alzheimer’s disease. We show that cleavage of tau by the 20S proteasome is most efficient within the aggregation-prone repeat region of tau and generates both short, aggregation-deficient peptides and two long fragments containing residues 1 to 251 and 1 to 218. Phosphorylation of tau by the non-proline–directed Ca2+/calmodulin-dependent protein kinase II inhibits degradation by the 20S proteasome. Phosphorylation of tau by GSK3β, a major proline-directed tau kinase, modulates tau degradation kinetics in a residue-specific manner. The study provides detailed insights into the degradation products of tau generated by the 20S proteasome, the residue specificity of degradation, single-residue degradation kinetics, and their regulation by posttranslational modification.
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000153283 7001_ $$00000-0002-6217-5450$$aFang, P.$$b1
000153283 7001_ $$0P:(DE-2719)2812657$$aIbanez de Opakua, Alain$$b2
000153283 7001_ $$00000-0003-3444-0947$$aHenneberg, F.$$b3
000153283 7001_ $$00000-0003-1888-6666$$aGodec, A.$$b4
000153283 7001_ $$00000-0001-6974-5324$$aPan, K.-T.$$b5
000153283 7001_ $$0P:(DE-2719)2812201$$aCima Omori, Maria Sol$$b6$$udzne
000153283 7001_ $$00000-0001-6220-9828$$aChari, A.$$b7
000153283 7001_ $$0P:(DE-2719)2541671$$aMandelkow, Eckhard$$b8
000153283 7001_ $$aUrlaub, H.$$b9
000153283 7001_ $$0P:(DE-2719)2810591$$aZweckstetter, Markus$$b10$$eLast author
000153283 773__ $$0PERI:(DE-600)2810933-8$$a10.1126/sciadv.aba3916$$gVol. 6, no. 30, p. eaba3916 -$$n30$$peaba3916 -$$tScience advances$$v6$$x2375-2548$$y2020
000153283 8564_ $$uhttps://advances.sciencemag.org/content/6/30/eaba3916
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