Open AccessInhibition of Protein Kinase CK2 Closes the CFTR Cl<sup>-</sup> Channel, but has no Effect on the Cystic Fibrosis Mutant ΔF508-CFTR
Author(s) -
KJ Treharne,
Zhe Xu,
J Chen,
O. Giles Best,
D.M. Cassidy,
D. C. Gruenert,
Péter Hegyi,
Michael A. Gray,
David N. Sheppard,
Karl Kunzelmann,
Anil Mehta
Publication year - 2009
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000257427
Subject(s) - δf508 , cystic fibrosis transmembrane conductance regulator , cystic fibrosis , apical membrane , chloride channel , microbiology and biotechnology , biology , xenopus , chemistry , biochemistry , membrane , genetics , gene
Deletion of phenylalanine-508 (DeltaF508) from the first nucleotide-binding domain (NBD1) in the wild-type cystic fibrosis (CF) transmembrane-conductance regulator (wtCFTR) causes CF. However, the mechanistic relationship between DeltaF508-CFTR and the diversity of CF disease is unexplained. The surface location of F508 on NBD1 creates the potential for protein-protein interactions and nearby, lies a consensus sequence (SYDE) reported to control the pleiotropic protein kinase CK2.