Casein kinase 2 specifically binds to and phosphorylates the carboxy termini of ENaC subunits
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....
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| Published in | European journal of biochemistry Vol. 269; no. 18; pp. 4551 - 4558 |
|---|---|
| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
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Oxford, UK
Blackwell Science Ltd
01.09.2002
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| Abstract | 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., 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 βT613 and γT623 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 βS631, a well‐conserved serine on the β subunit. Such phosphorylation is observed both in vitro using glutathione‐S‐transferase–ENaC fusion proteins and in vivo in ENaC‐expressing Xenopus oocytes. The γ subunit is weakly phosphorylated by this protein kinase on another residue (γT599), and the C tail of α is not significantly phosphorylated by this kinase. Thus, CK2 may be involved in the regulation of the epithelial Na+ channel. |
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| AbstractList | 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., 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 βT613 and γT623 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 βS631, a well‐conserved serine on the β subunit. Such phosphorylation is observed both in vitro using glutathione‐S‐transferase–ENaC fusion proteins and in vivo in ENaC‐expressing Xenopus oocytes. The γ subunit is weakly phosphorylated by this protein kinase on another residue (γT599), and the C tail of α is not significantly phosphorylated by this kinase. Thus, CK2 may be involved in the regulation of the epithelial Na+ channel. 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., 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 βT613 and γT623 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 βS631, a well‐conserved serine on the β subunit. Such phosphorylation is observed both in vitro using glutathione‐S‐transferase–ENaC fusion proteins and in vivo in ENaC‐expressing Xenopus oocytes. The γ subunit is weakly phosphorylated by this protein kinase on another residue (γT599), and the C tail of α is not significantly phosphorylated by this kinase. Thus, CK2 may be involved in the regulation of the epithelial Na + channel. 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., 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 βT613 and γT623 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 βS631, a well-conserved serine on the β subunit. Such phosphorylation is observed both in vitro using glutathione-S-transferase-ENaC fusion proteins and in vivo in ENaC-expressing Xenopus oocytes. The γ subunit is weakly phosphorylated by this protein kinase on another residue (γT599), and the C tail of α is not significantly phosphorylated by this kinase. Thus, CK2 may be involved in the regulation of the epithelial Na+ channel. 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. 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.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. |
| Author | Shi, Haikun Yung, Yuval Garty, Haim Asher, Carol Kligman, Luba Seger, Rony Reuveny, Eitan |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/12230567$$D View this record in MEDLINE/PubMed |
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| Snippet | A number of findings have suggested the involvement of protein phosphorylation in the regulation of the epithelial Na+ channel (ENaC). A recent study has... A number of findings have suggested the involvement of protein phosphorylation in the regulation of the epithelial Na + channel (ENaC). A recent study has... |
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| SubjectTerms | 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 |
| Title | Casein kinase 2 specifically binds to and phosphorylates the carboxy termini of ENaC subunits |
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