Casein kinase 2 specifically binds to and phosphorylates the carboxy termini of ENaC subunits

• Published in: European journal of biochemistry Vol. 269; no. 18; pp. 4551 - 4558
• Main Authors: Shi, Haikun, Asher, Carol, Yung, Yuval, Kligman, Luba, Reuveny, Eitan, Seger, Rony, Garty, Haim
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Science Ltd 01.09.2002
• Subjects: Amino Acid Sequence; Animals; casein; casein kinase 2; Casein Kinase II; ENaC; epithelial Na+ channel; Epithelial Sodium Channels; Glutathione Transferase - metabolism; mitogen-activated protein kinase; Molecular Sequence Data; Oocytes; Phosphorylation; Protein Binding; protein phosphorylation; Protein-Serine-Threonine Kinases - metabolism; Sequence Alignment; serine; sodium; Sodium Channels - metabolism; Xenopus

A number of findings have suggested the involvement of protein phosphorylation in the regulation of the epithelial Na+ channel (ENaC). A recent study has demonstrated that the C tails of the β and γ subunits of ENaC are subject to phosphorylation by at least three protein kinases [Shi, H., Asher, C....