HSPA1A-independent suppression of PARK2 C289G protein aggregation by human small heat shock proteins.

Molecular and cellular biology (2014-07-16)
Melania Minoia, Corien Grit, Harm H Kampinga
RESUMO

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.

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Sigma-Aldrich
Guanine, 98%
Sigma-Aldrich
Cytosine, ≥99%
Supelco
Guanine, Pharmaceutical Secondary Standard; Certified Reference Material
Sigma-Aldrich
Guanine, BioUltra
Supelco
Cytosine, Pharmaceutical Secondary Standard; Certified Reference Material
Gemcitabine impurity A, European Pharmacopoeia (EP) Reference Standard