Small heat shock proteins, protein degradation and protein aggregation diseases.
Small heat shock proteins have been characterized in vitro as ATP-independent molecular chaperones that can prevent aggregation of un- or mis-folded 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.
Department of Cell Biology, Section for Radiation and Stress Cell Biology, University Medical Center Groningen, Groningen, The Netherlands.
Michel J
MJ
Vos
Marianne P
MP
Zijlstra
Serena
S
Carra
Ody C M
OC
Sibon
Harm H
HH
Kampinga
D000199:Actins / Q000378:metabolism; D000818:Animals; D004331:Drosophila melanogaster; D050888:Heat-Shock Proteins, Small / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D019636:Neurodegenerative Diseases / Q000473:pathology*; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D020836:Protein Structure, Quaternary
D000199:Actins; D050888:Heat-Shock Proteins, Small; D010455:Peptides; C097188:polyglutamine