Home > Publications Database > Proteasomal degradation of the intrinsically disordered protein tau at single-residue resolution > print

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100 1 _ |a Ukmar-Godec, Tina
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245 _ _ |a Proteasomal degradation of the intrinsically disordered protein tau at single-residue resolution
260 _ _ |a Washington, DC [u.a.]
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520 _ _ |a Intrinsically 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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700 1 _ |a Fang, P.
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700 1 _ |a Ibanez de Opakua, Alain
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700 1 _ |a Henneberg, F.
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700 1 _ |a Godec, A.
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700 1 _ |a Pan, K.-T.
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700 1 _ |a Cima Omori, Maria Sol
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700 1 _ |a Chari, A.
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700 1 _ |a Mandelkow, Eckhard
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700 1 _ |a Urlaub, H.
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700 1 _ |a Zweckstetter, Markus
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