Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro

Wenbo Zhou, Chunmei Long, Anthony L. Fink, Vladimir N. Uversky

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

α-Synuclein, a natively unfolded protein aggregation which is implicated in the pathogenesis of Parkinson's disease and several other neurodegenerative diseases, is known to interact with a great number of unrelated proteins. Some of these proteins, such as β-synuclein and DJ-1, were shown to inhibit α-synuclein aggregation in vitro and in vivo therefore acting as chaperones. Since calbindin-D28K is co-localized with Ca2+ neuronal membrane pumps, and since α-synuclein is also found in the membrane proximity, these two proteins can potentially interact in vivo. Here we show that calbindin-D28K interacts with α-synuclein and inhibits its fibrillation in a calcium-dependent manner, therefore potentially acting as a calcium-dependent chaperone.

Original languageEnglish (US)
Pages (from-to)11-20
Number of pages10
JournalCentral European Journal of Biology
Volume5
Issue number1
DOIs
StatePublished - Jan 1 2010

Keywords

  • Aggregation
  • Fibrillation
  • Intrinsically disordered protein
  • Parkinson's disease
  • α-synuclein

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