Article

The small heat shock proteins family: the long forgotten chaperones.

Heat Shock Proteins and Cancer, INSERM UMR 866, Faculty of Medicine, Dijon, France.
The international journal of biochemistry & cell biology (impact factor: 4.89). 03/2012; 44(10):1588-92. DOI:10.1016/j.biocel.2012.02.022 pp.1588-92
Source: PubMed

ABSTRACT Small heat shock proteins are a rather heterogeneous family of ATP-independent chaperones, some of which have been proven to block protein aggregation and help the cells to survive stressful conditions. Although much less studied than high molecular weight HSPs like HSP70/HSPA or HSP90/HSPC, their implication in physio-pathological processes and human diseases is now well evidenced, as it will be discussed in the different reviews of this special issue. In this mini-review we will just present a general introduction about the small heat shock proteins family. This article is part of a Directed Issue entitled: Small HSPs in physiology and pathology.

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    Article: A chaperone trap contributes to the onset of cystic fibrosis.
    Judith A Coppinger, Darren M Hutt, Abbas Razvi, Atanas V Koulov, Sandra Pankow, John R Yates, William E Balch
    [show abstract] [hide abstract]
    ABSTRACT: Protein folding is the primary role of proteostasis network (PN) where chaperone interactions with client proteins determine the success or failure of the folding reaction in the cell. We now address how the Phe508 deletion in the NBD1 domain of the cystic fibrosis (CF) transmembrane conductance regulator (CFTR) protein responsible for cystic fibrosis (CF) impacts the binding of CFTR with cellular chaperones. We applied single ion reaction monitoring mass spectrometry (SRM-MS) to quantitatively characterize the stoichiometry of the heat shock proteins (Hsps) in CFTR folding intermediates in vivo and mapped the sites of interaction of the NBD1 domain of CFTR with Hsp90 in vitro. Unlike folding of WT-CFTR, we now demonstrate the presence of ΔF508-CFTR in a stalled folding intermediate in stoichiometric association with the core Hsps 40, 70 and 90, referred to as a 'chaperone trap'. Culturing cells at 30 C resulted in correction of ΔF508-CFTR trafficking and function, restoring the sub-stoichiometric association of core Hsps observed for WT-CFTR. These results support the interpretation that ΔF508-CFTR is restricted to a chaperone-bound folding intermediate, a state that may contribute to its loss of trafficking and increased targeting for degradation. We propose that stalled folding intermediates could define a critical proteostasis pathway branch-point(s) responsible for the loss of function in misfolding diseases as observed in CF.
    PLoS ONE 01/2012; 7(5):e37682. · 4.09 Impact Factor
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Keywords

different reviews
 
Directed Issue
 
general introduction
 
human diseases
 
molecular weight HSPs
 
Small heat shock proteins
 
small heat shock proteins family
 
special issue
 
stressful conditions