Regulation of tyrosine hydroxylase is preserved across different homo- and heterodimeric 14-3-3 proteins

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• 作者：Sadaf Ghorbani ; Agnete Fossbakk ; Ana Jorge-Finnigan ; Marte I. Flydal…
• 关键词：14 ; 3 ; 3 ; Heterodimer ; Isoform ; Tyrosine hydroxylase ; Activation
• 刊名：Amino Acids
• 出版年：2016
• 出版时间：May 2016
• 年：2016
• 卷：48
• 期：5
• 页码：1221-1229
• 全文大小：1,248 KB
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• 作者单位：Sadaf Ghorbani (1) (2)
  Agnete Fossbakk (1) (2)
  Ana Jorge-Finnigan (1) (2)
  Marte I. Flydal (1)
  Jan Haavik (1) (2) (3)
  Rune Kleppe (1) (2)
  
  1. Department of Biomedicine, University of Bergen, Bergen, Norway
  2. K.G. Jebsen Centre for Neuropsychiatric Disorders, University of Bergen, Bergen, Norway
  3. Haukeland University Hospital, Bergen, Norway
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Analytical Chemistry
  Biochemical Engineering
  Life Sciences
  Proteomics
  Neurobiology
  
• 出版者：Springer Wien
• ISSN：1438-2199
• 卷排序：48

文摘

Tyrosine hydroxylase (TH) is regulated by members of the 14-3-3 protein family. However, knowledge about the variation between 14-3-3 proteins in their regulation of TH is still limited. We examined the binding, effects on activation and dephosphorylation kinetics of tyrosine hydroxylase (TH) by abundant midbrain 14-3-3 proteins (β, η, ζ, γ and ε) of different dimer composition. All 14-3-3 homodimers and their respective 14-3-3ε-heterodimers bound with similar high affinity (K _d values of 1.4–3.8 nM) to serine19 phosphorylated human TH (TH-pS19). We similarly observed a consistent activation of bovine (3.3- to 4.4-fold) and human TH-pS19 (1.3–1.6 fold) across all the different 14-3-3 dimer species, with homodimeric 14-3-3γ being the strongest activator. Both hetero- and homodimers of 14-3-3 strongly inhibited dephosphorylation of TH-pS19, and we speculate if this is an important homeostatic mechanism of 14-3-3 target-protein regulation in vivo. We conclude that TH is a robust interaction partner of different 14-3-3 dimer types with moderate variability between the 14-3-3 dimers on their regulation of TH. Keywords 14-3-3 Heterodimer Isoform Tyrosine hydroxylase Activation