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*

*Corresponding author for this work

    Research output: Contribution to journalEditorialAcademicpeer-review

    37 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)101-103
    Number of pages3
    Issue number1
    Publication statusPublished - Jan-2011


    • heat shock protein
    • HSPB
    • polyglutamine diseases
    • autophagy
    • Hsp70

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