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Insulin-degrading enzyme is activated by the C-terminus of alpha-synuclein
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
2015 (engelsk)Inngår i: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 466, nr 2, s. 192-195Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The insulin-degrading enzyme (IDE) plays a key role in type-2 diabetes and typically degrades small peptides such as insulin, amyloid beta and islet amyloid polypeptide. We recently reported a novel non-proteolytical interaction in vitro between IDE and the Parkinson's disease 140-residue protein alpha-synuclein that resulted in dual effects: arrested alpha-synuclein oligomers and, simultaneously, increased IDE proteolysis activity. Here we demonstrate that these outcomes arise due to IDE interactions with the C-terminus of alpha-synuclein. Whereas a peptide containing the first 97 residues of alpha-synuclein did not improve IDE activity and its aggregation was not blocked by IDE, a peptide with the C-terminal 44 residues of alpha-synuclein increased IDE proteolysis to the same degree as full-length alpha-synuclein. Because the alpha-synuclein C-terminus is acidic, the interaction appears to involve electrostatic attraction with IDE's basic exosite, known to be involved in activation.

sted, utgiver, år, opplag, sider
2015. Vol. 466, nr 2, s. 192-195
Emneord [en]
Insulin degrading enzyme, Parkinson's disease, alpha-Synuclein, Amyloid, Proteolysis
HSV kategori
Identifikatorer
URN: urn:nbn:se:umu:diva-110991DOI: 10.1016/j.bbrc.2015.09.002ISI: 000362610800008PubMedID: 26343304OAI: oai:DiVA.org:umu-110991DiVA, id: diva2:872237
Tilgjengelig fra: 2015-11-18 Laget: 2015-11-02 Sist oppdatert: 2018-06-07bibliografisk kontrollert

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