CFTR: new members join the fold.
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.
Skach
William R
WR
Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, OR 97239, USA. skachw@ohsu.edu
D000818:Animals; D006224:Cricetinae; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000737:chemistry* / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D050505:Mutant Proteins / Q000378:metabolism; D017510:Protein Folding; D021381:Protein Transport; D034741:RNA, Small Interfering / Q000378:metabolism
D018841:HSP90 Heat-Shock Proteins; D050505:Mutant Proteins; D034741:RNA, Small Interfering; D019005:Cystic Fibrosis Transmembrane Conductance Regulator