Regulation of hERG and hEAG channels by Src and by SHP-1 tyrosine phosphatase via an ITIM region in the cyclic nucleotide binding domain

• Main Authors: Schlichter L.C., Jiang J., Wang J., Newell E.W., Tsui F.W.L., Lam D.
• Other Authors: MICROBIOLOGY AND IMMUNOLOGY
• Format: Article
• Published: Public Library of Science 2020
• Subjects: cyclic nucleotide; potassium channel; potassium channel hEAG; potassium channel HERG; protein tyrosine kinase; protein tyrosine phosphatase SHP 1; unclassified drug; amino acid sequence; article; controlled study; enzyme activation; enzyme activity; human; human cell; immunoreceptor tyrosine based inhibition motif; nucleotide binding site; nucleotide sequence; potassium current; protein phosphorylation; regulatory mechanism; Action Potentials; Amino Acid Sequence; Animals; Conserved Sequence; Cyclic AMP; Ether-A-Go-Go Potassium Channels; Gene Expression Regulation; HEK293 Cells; Humans; Mice; Molecular Sequence Data; Patch-Clamp Techniques; Peptides; Protein Binding; Protein Structure, Tertiary; Protein Tyrosine Phosphatase, Non-Receptor Type 6; Pyrazoles; Pyrimidines; Rats; Sequence Homology, Amino Acid; Signal Transduction; src-Family Kinases
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/165956
• Institution: National University of Singapore

10.1371/journal.pone.0090024