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doi: 10.1016/j.cell.2006.11.002.
CFTR: new members join the fold
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- PMID: 17110327
- DOI: 10.1016/j.cell.2006.11.002
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CFTR: new members join the fold
Cell.
.
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Abstract
The folding, misfolding, and degradation of membrane proteins is controlled by multiple processes within the cell. In this issue of Cell, Wang et al. (2006) present an interactome for CFTR, the chloride channel that is misfolded and prematurely degraded in cystic fibrosis. Among the proteins interacting with CFTR is a new member of the Hsp90 chaperone system, Aha1, that plays a central role in CFTR folding.
Comment on
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Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis.Cell. 2006 Nov 17;127(4):803-15. doi: 10.1016/j.cell.2006.09.043. Cell. 2006. PMID: 17110338
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