ArticleThe Journal of biological chemistry2009
Three-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranes.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 45 citations in OpenAlex.
- Tyrosine Hydroxylase Deficiency Impairs TH Axonal Transport, Brain Function, and Neuronal Plasticity.Journal of inherited metabolic disease · 2026Article
- Article
- Versatility of 14-3-3 proteins and their roles in bone and joint-related diseases.Bone research · 2024Review
- 14-3-3 proteins-a moonlight protein complex with therapeutic potential in neurological disorder: in-depth review with Alzheimer's disease.Frontiers in molecular biosciences · 2024Review
- Investigating the Disordered and Membrane-Active Peptide A-Cage-C Using Conformational Ensembles.Molecules (Basel, Switzerland) · 2021Article
- Relevance of Electrostatics for the Interaction of Tyrosine Hydroxylase with Porous Silicon Nanoparticles.Molecular pharmaceutics · 2021Article
- Involvement of the 14-3-3 Gene Family in Autism Spectrum Disorder and Schizophrenia: Genetics, Transcriptomics and Functional Analyses.Journal of clinical medicine · 2020Article
- iPSC modeling of young-onset Parkinson's disease reveals a molecular signature of disease and novel therapeutic candidates.Nature medicine · 2020Article
- Downregulation of 14-3-3 Proteins in Alzheimer's Disease.Molecular neurobiology · 2020Article
- Phosphorylation at serine 31 targets tyrosine hydroxylase to vesicles for transport along microtubules.The Journal of biological chemistry · 2017Article
- Tyrosine Hydroxylase Binding to Phospholipid Membranes Prompts Its Amyloid Aggregation and Compromises Bilayer Integrity.Scientific reports · 2016Article
- Regulation of tyrosine hydroxylase is preserved across different homo- and heterodimeric 14-3-3 proteins.Amino acids · 2016Article
- Dysregulated 14-3-3 Family in Peripheral Blood Leukocytes of Patients with Schizophrenia.Scientific reports · 2016Article
- Identification of chaperones in a MPPAmerican journal of translational research · 2016Article
- Complex molecular regulation of tyrosine hydroxylase.Journal of neural transmission (Vienna, Austria : 1996) · 2014Review
- Phosphorylation dependence and stoichiometry of the complex formed by tyrosine hydroxylase and 14-3-3γ.Molecular & cellular proteomics : MCP · 2014Article
- Sustained N-methyl-d-aspartate receptor hypofunction remodels the dopamine system and impairs phasic signaling.The European journal of neuroscience · 2014Article
- Identification of a novel lytic peptide for the treatment of solid tumours.Genes & cancer · 2014Article
- The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes.Journal of molecular biology · 2014Article
- Locomotor hyperactivity in 14-3-3ζ KO mice is associated with dopamine transporter dysfunction.Translational psychiatry · 2013Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tyrosine hydroxylase (TH), the rate-limiting enzyme in the synthesis of catecholamines, is activated by phosphorylation-dependent binding to 14-3-3 proteins. The N-terminal domain of TH is also involved in interaction with lipid membranes. We investigated the binding of the N-terminal domain to its different partners, both in the unphosphorylated (TH-(1-43)) and Ser(19)-phosphorylated (THp-(1-43)) states by surface plasmon resonance. THp-(1-43) showed high affinity for 14-3-3 proteins (K(d) approximately 0.5 microM for 14-3-3gamma and -zeta and 7 microM for 14-3-3eta). The domains also bind to negatively charged membranes with intermediate affinity (concentration at half-maximal binding S(0.5) = 25-58 microM (TH-(1-43)) and S(0.5) = 135-475 microM (THp-(1-43)), depending on phospholipid composition) and concomitant formation of helical structure. 14-3-3gamma showed a preferential binding to membranes, compared with 14-3-3zeta, both in chromaffin granules and with liposomes at neutral pH. The affinity of 14-3-3gamma for negatively charged membranes (S(0.5) = 1-9 microM) is much higher than the affinity of TH for the same membranes, compatible with the formation of a ternary complex between Ser(19)-phosphorylated TH, 14-3-3gamma, and membranes. Our results shed light on interaction mechanisms that might be relevant for the modulation of the distribution of TH in the cytoplasm and membrane fractions and regulation of L-DOPA and dopamine synthesis.
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