Cited by 95Protein Kinase Regulation and GTPase Signaling14-3-3 protein interactionsProtein Tyrosine Phosphatases

Regulation of tyrosine hydroxylase by stress-activated protein kinases

Open access
Toska, Karen, Kleppe, Rune, Armstrong, Christopher G., Morrice, Nick A., Cohen, Philip, Haavik, Jan·2002·Journal of Neurochemistry

Abstract

Recombinant human tyrosine hydroxylase (hTH1) was found to be phosphorylated by mitogen and stress‐activated protein kinase 1 (MSK1) at Ser40 and by p38 regulated/activated kinase (PRAK) on Ser19. Phosphorylation by MSK1 induced an increase in Vmax and a decrease in Km for 6‐(R)‐5,6,7,8‐tetrahydrobiopterin (BH 4), while these kinetic parameters were unaffected as a result of phosphorylation by PRAK. Phosphorylation of both Ser40 and Ser19 induced a high‐affinity binding of 14‐3‐3 proteins, but only the interaction of 14‐3‐3 with Ser19 increased the hTH1 activity. The 14‐3‐3 proteins also inhibited the rate of dephosphorylation of Ser19 and Ser40 by 82 and 36%, respectively. The phosphorylation of hTH1 on Ser19 caused a threefold increase in the rate of phosphorylation of Ser40. These studies provide new insights into the possible roles of stress‐activated protein kinases in the regulation of catecholamine biosynthesis.

Integrity signals

Registry

Crossref · 10.1046/j.1471-4159.2002.01172.x

Cites

39 of 39 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

The text we found for this paper looks like another document, so its claims and self-check weren’t run. The registry and citation checks still apply.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The text we found for this paper looks like another document, so the self-check wasn’t run.

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Toska, K., Kleppe, R., Armstrong, C. G., Morrice, N. A., Cohen, P., & Haavik, J.
Affiliations
  • University of Bergen (NO)
  • University of Dundee (GB)
Corresponding author
Toska, Karen
Venue
Journal of Neurochemistry
Publisher
Wiley
Published
2002-11
Volume
83
Issue
4
Pages
775-783
ISSN
  • 0022-3042 (ISSN-L)
  • 1471-4159
OpenAlex
W1536745609
Cited by
95
References
39
Citations by year
2023: 3 · 2022: 1 · 2021: 3 · 2020: 3 · 2019: 5 · 2018: 3 · 2017: 3 · 2016: 5 · 2015: 1 · 2014: 3 · 2013: 6 · 2012: 3
FWCI
2.32
Type
journal article
Language
en
Open access
Locations
  • Journal of Neurochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • Discovery Research Portal (University of Dundee) (submittedVersion, other-oa)
Funders
  • Kreftforeningen
  • Universitetet i Bergen
  • Norges Forskningsråd
  • Medical Research Council
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 14-3-3 protein interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords
tyrosine hydroxylase, c-Jun N-terminal kinase, MSK1, p38 MAPK, protein phosphorylation, 14-3-3 proteins, tetrahydrobiopterin, enzyme kinetics, catecholamine synthesis, enzyme regulation
MeSH terms
MAP-Kinase-Activated Kinase 2, Amino Acid Sequence, Binding Sites, Chromatography, High Pressure Liquid, Circular Dichroism, Enzyme Activation, Enzyme Stability, Humans, Kinetics, Phosphorylation, Protein Binding, Substrate Specificity, Temperature, Tyrosine 3-Monooxygenase, Protein Serine-Threonine Kinases, Cyclic AMP-Dependent Protein Kinases, Mitogen-Activated Protein Kinase 1, Surface Plasmon Resonance, Ribosomal Protein S6 Kinases, 90-kDa, Intracellular Signaling Peptides and Proteins, 14-3-3 Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review