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

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.

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 Creators:
Szellas, Tanjef1, Author           
Nagel, Georg1, Author           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              

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Free keywords: Cystic fibrosis transmembrane conductance regulator; Phosphorylation site; Membrane-bound phosphatase; ATP dependence; Phosphatase
 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.

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Language(s): -
 Dates: 2002-12-232002-11-212002-12-232003-01-102003
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/s0014-5793(02)03892-9
PMID: 12560093
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 535 (1-3) Sequence Number: - Start / End Page: 141 - 146 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501