Abstract:
:Small heat shock proteins (sHsps) are ubiquitous molecular chaperones that are implicated in a variety of diseases. Upon stress, they stabilize unfolding proteins and prevent them from aggregating. However, under physiological conditions without severe stress, some sHsps interact with other proteins. In a perspective view, their ability to bind specific client proteins might allow them to fine-tune the availability of the client for other, client-dependent cellular processes. Additionally, some sHsps seem to interact with specific co-chaperones. These co-chaperones are usually part of large protein machineries that are functionally modulated upon sHsps interaction. Finally, secreted human sHsps seem to interact with receptor proteins, potentially as signal molecules transmitting the stress status from one cell to another. This review focuses on the mechanistic description of these different binding modes for human sHsps and how this might help to understand and modulate the function of sHsps in the context of disease.
journal_name
Expert Rev Proteomicsjournal_title
Expert review of proteomicsauthors
Mymrikov EV,Haslbeck Mdoi
10.1586/14789450.2015.1039993subject
Has Abstractpub_date
2015-06-01 00:00:00pages
295-308issue
3eissn
1478-9450issn
1744-8387journal_volume
12pub_type
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journal_title:Expert review of proteomics
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journal_title:Expert review of proteomics
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