HSPA1A-Independent Suppression of PARK2 C289G Protein Aggregation by Human Small Heat Shock Proteins

Melania Minoia, Corien Grit, Harm H. Kampinga*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

7 Citations (Scopus)
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Abstract

The C289G mutation of the parkin E3-ubiquitin protein ligase (PARK2) is associated with autosomal recessive juvenile onset Parkinson's disease and was found to be associated with protein aggregation. Members of the human small heat shock proteins (HSPBs) have been implicated in protein degradation and prevention of protein aggregation. In this study, we show that of the 10 HSPB members, individual overexpression of HSPB1, HSPB2, HSPB4, and HSPB7 suppresses PARK2 C289G-associated protein aggregation. Intriguingly, the protective actions of these HSPBs are not impaired upon inactivation of the ATP-dependent HSP70 chaperone machines. Depending on the HSPB member the protective actions involve either autophagic or proteasomal degradation pathways.

Original languageEnglish
Pages (from-to)3570-3578
Number of pages9
JournalMolecular and Cellular Biology
Volume34
Issue number19
Early online date14-Jul-2014
DOIs
Publication statusPublished - Oct-2014

Keywords

  • RECESSIVE JUVENILE PARKINSONISM
  • ALPHA-B-CRYSTALLIN
  • IN-VITRO
  • PROTEASOMAL DEGRADATION
  • MULTICHAPERONE NETWORK
  • MOLECULAR CHAPERONES
  • MUTATIONS
  • DISEASE
  • CELLS
  • HSP27

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