Related Experiment Video
Updated: Mar 29, 2026

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
Published on: May 20, 2020
Potential sites of CFTR activation by tyrosine kinases
Arnaud Billet1,2, Yanlin Jia1,2, Timothy J Jensen3
1a Department of Physiology , McGill University , Montreal , Quebec , Canada.
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.
Related Concept Videos
Receptor Tyrosine Kinases
Enzyme-linked Receptors
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Transducer Mechanism: Enzyme-Linked Receptors
Major types that are helpful drug targets include:
Intracellular Signaling Affects Focal Adhesions
Some...
MAPK Signaling Cascades
Amplifying Signals via Enzymatic Cascade

