English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons137913

Szellas,  Tanjef
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137819

Nagel,  Georg
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Szellas, T., & Nagel, G. (2003). Apparent affinity of CFTR for ATP is increased by continuous kinase activity. FEBS Letters, 535(1-3), 141-146. doi:10.1016/s0014-5793(02)03892-9.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DBE0-9
Abstract
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.