Journal
CHANNELS
Volume 10, Issue 3, Pages 247-251Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/19336950.2015.1126010
Keywords
CFTR regulation; cystic fibrosis; phosphotyrosine; Pyk2; Src
Categories
Funding
- NIH
- CIHR
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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.
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