Small heat shock proteins, protein degradation and protein aggregation diseases

Michel J. Vos, Marianne P. Zijlstra, Serena Carra, Ody C. M. Sibon, Harm H. Kampinga*

*Bijbehorende auteur voor dit werk

    OnderzoeksoutputAcademicpeer review

    38 Citaten (Scopus)

    Samenvatting

    Small heat shock proteins have been characterized in vitro as ATP-independent molecular chaperones that can prevent aggregation of un- or misfolded proteins and assist in their refolding with the help of ATP-dependent chaperone machines (e. g., the Hsp70 proteins). Comparison of the functionality of the 10 human members of the small HSPB family in cell models now reveals that some members function entirely differently and independently from Hsp70 machines. One member, HSPB7, has strong activities to prevent toxicity of polyglutamine-containing proteins in cells and Drosophila, and seems to act by assisting the loading of misfolded proteins or small protein aggregates into autophagosomes.

    Originele taal-2English
    Pagina's (van-tot)101-103
    Aantal pagina's3
    TijdschriftAutophagy
    Volume7
    Nummer van het tijdschrift1
    DOI's
    StatusPublished - jan-2011

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