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Protein kinase A phosphorylates and regulates dimerization of 14-3-3ζ
- Title
- Protein kinase A phosphorylates and regulates dimerization of 14-3-3ζ
- Authors
- Gu Y.-M.; Jin Y.-H.; Choi J.-K.; Baek K.-H.; Yeo C.-Y.; Lee K.-Y.
- Ewha Authors
- 여창열
- SCOPUS Author ID
- 여창열
- Issue Date
- 2006
- Journal Title
- FEBS Letters
- ISSN
- 0014-5793
- Citation
- FEBS Letters vol. 580, no. 1, pp. 305 - 310
- Indexed
- SCI; SCIE; SCOPUS
- Document Type
- Article
- Abstract
- Recognition of phosphorylated serine/threonine-containing motifs by 14-3-3 depends on the dimerization of 14-3-3. However, the molecular cues that control 14-3-3 dimerization are not well understood. In order to identify proteins that control 14-3-3 dimerization, we analyzed proteins that have effects on 14-3-3 dimerization and report that protein kinase A (PKA) phosphorylates 14-3-3ζ at a specific residue (Ser58). Phosphorylation by PKA leads to modulation of 14-3-3ζ dimerization and affect its interaction with partner proteins. Substitution of Ser58 to Ala completely abolished phosphorylation of 14-3-3ζ by PKA. A phospho-mimic mutant of 14-3-3ζ, Ser58 to Glu substitution, failed to form homodimers, showed reduced interaction with 14-3-3ε and p53, and could not enhance transcriptional activity of p53. Moreover, activation of PKA decreases and inhibition of PKA increases the dimerization of 14-3-3ζ and the functional interaction of 14-3-3ζ with p53. Therefore, our results suggest that PKA is a new member of protein kinases that can phosphorylate and impair the function of 14-3-3. © 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
- DOI
- 10.1016/j.febslet.2005.12.024
- Appears in Collections:
- 자연과학대학 > 생명과학전공 > Journal papers
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