Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle

Article Abstract:

The Hsc70-interacting protein Hip is involved in the regulation of the eukaryotic 70 kDa Hsc70 (heat shock cognate 70). Hip binds the ATPase regions of Hsp40 activated-Hsp70 molecules. This binding stabilizes the ADP form of Hsp70. The mechanism is different from the control of Hsp70 in bacteria cytosol as it does not involve a GrpE-like nucleotide exchange factor. Hip also controls the synthesis and structural changes in proteins that interact with Hsp70 and Hsp90. Hip functions as a molecular chaperone in an ATP-independent manner.

Research, Proteins, Heat shock proteins, Adenosine triphosphate, ATP

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Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis

Article Abstract:

Proteomics is used to assess global cystic fibrosis (CF) transmembrane conductance regulator (CFTR) protein interactions in order to show that Hsp90 cochaperones modulate Hsp90-dependent stability of CFTR protein folding in the endoplasmic reticulum (ER). The results have shown that the cellular chaperone pool does not simply prevent aggregation but also contributes to local folding environments by controlling the success or failure of the protein fold for function and export.

Usage, Endoplasmic reticulum, Proteomics

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CFTR: New members join the fold

Article Abstract:

New factors are identified that govern the fate of the cystic fibrosis transmembrane conductance regulator (CFTR), an apical membrane adenosine triphosphate (ATP)-regulated chloride channel whose misfolding is implicated in cystic fibrosis. The results have shown that manipulating the Hsp70 and Hsp90 dsystems can boost the maturation of some proteins that are prone to misfolding, which plays central role in CFTR folding.

Molecular chaperones

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