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Eur J Biochem 2002 Sep 01;26918:4551-8. doi: 10.1046/j.1432-1033.2002.03154.x.
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Casein kinase 2 specifically binds to and phosphorylates the carboxy termini of ENaC subunits.

Shi H , Asher C , Yung Y , Kligman L , Reuveny E , Seger R , Garty H .

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 beta and gamma subunits of ENaC are subject to phosphorylation by at least three protein kinases [Shi, H., Asher, C., Chigaev, A., Yung, Y., Reuveny, E., Seger, R. & Garty, H. (2002) J. Biol. Chem. 277, 13539-13547]. One of them was identified as ERK which phosphorylates betaT613 and gammaT623 and affects the channel interaction with Nedd4. The current study identifies a second protein kinase as casein kinase 2 (CK2), or CK-2-like kinase. It phosphorylates betaS631, a well-conserved serine on the beta subunit. Such phosphorylation is observed both in vitro using glutathione-S-transferase-ENaC fusion proteins and in vivo in ENaC-expressing Xenopus oocytes. The gamma subunit is weakly phosphorylated by this protein kinase on another residue (gammaT599), and the C tail of alpha is not significantly phosphorylated by this kinase. Thus, CK2 may be involved in the regulation of the epithelial Na+ channel.

PubMed ID: 12230567
Article link: Eur J Biochem

Species referenced: Xenopus
Genes referenced: csnk2b mapk1 nedd4