dc.contributor.author | Ghorbani, Sadaf | en_US |
dc.contributor.author | Fossbakk, Agnete | en_US |
dc.contributor.author | Jorge Finnigan, Ana | en_US |
dc.contributor.author | Flydal, Marte Innselset | en_US |
dc.contributor.author | Haavik, Jan | en_US |
dc.contributor.author | Kleppe, Rune | en_US |
dc.date.accessioned | 2016-12-30T10:16:05Z | |
dc.date.available | 2016-12-30T10:16:05Z | |
dc.date.issued | 2016-05 | |
dc.Published | Amino Acids 2016, 48(5):1221-1229 | eng |
dc.identifier.issn | 1438-2199 | |
dc.identifier.uri | https://hdl.handle.net/1956/15310 | |
dc.description.abstract | 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 (Kd 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. | en_US |
dc.language.iso | eng | eng |
dc.publisher | Springer | eng |
dc.rights | Attribution CC BY | eng |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | eng |
dc.subject | 14-3-3 | eng |
dc.subject | Heterodimer | eng |
dc.subject | Isoform | eng |
dc.subject | Tyrosine hydroxylase | eng |
dc.subject | Activation | eng |
dc.title | Regulation of tyrosine hydroxylase is preserved across different homo- and heterodimeric 14-3-3 proteins | en_US |
dc.type | Peer reviewed | |
dc.type | Journal article | |
dc.date.updated | 2016-12-13T13:46:54Z | |
dc.description.version | publishedVersion | en_US |
dc.rights.holder | Copyright 2016 The Author(s) | |
dc.identifier.doi | https://doi.org/10.1007/s00726-015-2157-0 | |
dc.identifier.cristin | 1366118 | |