Potential sites of CFTR activation by tyrosine kinases

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 res...

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Bibliographic Details
Published in:Channels (Austin, Tex.) Tex.), 2016-01, Vol.10 (3), p.247-251
Main Authors: Billet, Arnaud, Jia, Yanlin, Jensen, Timothy J., Hou, Yue-Xian, Chang, Xiu-Bao, Riordan, John R., Hanrahan, John W.
Format: Article
Language:English
Subjects:
Addendum
Animals
Cell Line
Cellular Biology
CFTR regulation
Cricetinae
cystic fibrosis
Cystic Fibrosis Transmembrane Conductance Regulator - genetics
Cystic Fibrosis Transmembrane Conductance Regulator - metabolism
Electrophysiological Phenomena
Enzyme Activation
Life Sciences
Mutagenesis, Site-Directed
Mutation
phosphotyrosine
Protein-Tyrosine Kinases - metabolism
Pyk2
Src
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Summary: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.
ISSN:1933-6950
1933-6969
DOI:10.1080/19336950.2015.1126010