Clusterin is a ubiquitous glycoprotein found in most physiological fluids and tissues. Although not fully understood, the function of clusterin seems to be related to its ability to bind a wide variety of molecules. Since clusterin has been found associated with extracellular protein aggregates, a role as a molecular chaperone has been proposed. In this issue of the Biochemical Journal, Le Dréan and colleagues demonstrate an up-regulation of clusterin in neuronal cells exposed to proteotoxic stress that results in unfolded protein accumulation and proteasome impairment, both commonly associated with neurodegenerative diseases. Interestingly, expression of clusterin was found to be regulated by two members of the HSF (heat-shock factor) family, HSF1 and HSF2, which possibly form a trimeric complex on the clusterin promoter. The study proposes clusterin as a player in a cellular defence mechanism against harmful protein accumulation, and highlights the importance of elucidating further the exact role of clusterin and the intriguing interaction between HSF1 and HSF2.
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March 15 2006
Clustering of heat-shock factors
Johanna K. Björk;
Johanna K. Björk
1Department of Biology, Åbo Akademi University, Turku Centre for Biotechnology, Åbo Akademi University and University of Turku, FI-20521 Turku, Finland
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Lea Sistonen
Lea Sistonen
1
1Department of Biology, Åbo Akademi University, Turku Centre for Biotechnology, Åbo Akademi University and University of Turku, FI-20521 Turku, Finland
1To whom correspondence should be addressed (email lea.sistonen@btk.fi).
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Publisher: Portland Press Ltd
Received:
January 10 2006
Accepted:
January 12 2006
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London
2006
Biochem J (2006) 395 (1): e5.
Article history
Received:
January 10 2006
Accepted:
January 12 2006
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Citation
Johanna K. Björk, Lea Sistonen; Clustering of heat-shock factors. Biochem J 1 April 2006; 395 (1): e5. doi: https://doi.org/10.1042/BJ20060071
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