Potential sites of CFTR activation by tyrosine kinases

Arnaud Billet, Yanlin Jia, Timothy J. Jensen, Yue Xian Hou, Xiu Bao Chang, John R. Riordan, John W. Hanrahan

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

The CFTR chloride channel is tightly regulated by phosphorylation at multiple serine residues. Recently it has been proposed that its activity is also regulated by tyrosine kinases, however the tyrosine phosphorylation sites remain to be identified. In this study we examined 2 candidate tyrosine residues near the boundary between the first nucleotide binding domain and the R domain, a region which is important for channel function but devoid of PKA consensus sequences. Mutating tyrosines at positions 625 and 627 dramatically reduced responses to Src or Pyk2 without altering the activation by PKA, suggesting they may contribute to CFTR regulation.

Original languageEnglish (US)
Pages (from-to)247-251
Number of pages5
JournalChannels (Austin, Tex.)
Volume10
Issue number3
DOIs
StatePublished - Jan 1 2016

Keywords

  • CFTR regulation
  • Pyk2
  • Src
  • cystic fibrosis
  • phosphotyrosine

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

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  • Cite this

    Billet, A., Jia, Y., Jensen, T. J., Hou, Y. X., Chang, X. B., Riordan, J. R., & Hanrahan, J. W. (2016). Potential sites of CFTR activation by tyrosine kinases. Channels (Austin, Tex.), 10(3), 247-251. https://doi.org/10.1080/19336950.2015.1126010