Apparent affinity of CFTR for ATP is increased by continuous kinase activity

FEBS Letters

Szellas, Tanjef¹  Nagel, Georg¹ 

[1] Max-Planck-Institut für Biophysik, Kennedyallee 70, D-60596 Frankfurt/Main, Germany

关键词: Cystic fibrosis transmembrane conductance regulator;    Phosphorylation site;    Membrane-bound phosphatase;    ATP dependence;    Phosphatase;    CFTR;    cystic fibrosis transmembrane conductance regulator;    PKA;    cAMP-dependent protein kinase catalytic subunit;    cGK-II;    membrane-bound cGMP-dependent protein kinase;    bR;    bacteriorhodopsin;   

DOI  :  10.1016/S0014-5793(02)03892-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride channel which is activated by protein phosphorylation and nucleoside triphosphates. We demonstrate here that fusion of the soluble catalytic subunit of cAMP-dependent protein kinase to the membrane protein bacteriorhodopsin yields a constitutively active protein kinase which activates CFTR effectively. As it is membrane-bound it is particularly useful for continuous perfusion of excised inside-out patches. We also tested the effect of a naturally membrane-bound protein kinase, cGMP-dependent protein kinase II, on CFTR. Both kinases, when continuously active, increase apparent affinity of CFTR to ATP about two-fold emphasizing the role of phosphorylation in modulating the interaction of ATP with the nucleotide binding domains.

【 授权许可】

Unknown