Tryptophanemia is controlled by a tryptophan-sensing mechanism ubiquitinating tryptophan 2,3-dioxygenase.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
08 06 2021
Historique:
entrez: 2 6 2021
pubmed: 3 6 2021
medline: 15 12 2021
Statut: ppublish

Résumé

Maintaining stable tryptophan levels is required to control neuronal and immune activity. We report that tryptophan homeostasis is largely controlled by the stability of tryptophan 2,3-dioxygenase (TDO), the hepatic enzyme responsible for tryptophan catabolism. High tryptophan levels stabilize the active tetrameric conformation of TDO through binding noncatalytic exosites, resulting in rapid catabolism of tryptophan. In low tryptophan, the lack of tryptophan binding in the exosites destabilizes the tetramer into inactive monomers and dimers and unmasks a four-amino acid degron that triggers TDO polyubiquitination by SKP1-CUL1-F-box complexes, resulting in proteasome-mediated degradation of TDO and rapid interruption of tryptophan catabolism. The nonmetabolizable analog alpha-methyl-tryptophan stabilizes tetrameric TDO and thereby stably reduces tryptophanemia. Our results uncover a mechanism allowing a rapid adaptation of tryptophan catabolism to ensure quick degradation of excess tryptophan while preventing further catabolism below physiological levels. This ensures a tight control of tryptophanemia as required for both neurological and immune homeostasis.

Identifiants

pubmed: 34074763
pii: 2022447118
doi: 10.1073/pnas.2022447118
pmc: PMC8201853
pii:
doi:

Substances chimiques

alpha-methyltryptophan 13510-08-2
Tryptophan 8DUH1N11BX
Tryptophan Oxygenase EC 1.13.11.11

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Déclaration de conflit d'intérêts

Competing interest statement: B.J.V.d.E. is co-founder of iTeos Therapeutics.

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Auteurs

Simon Klaessens (S)

Ludwig Institute for Cancer Research, 1200 Brussels, Belgium.
de Duve Institute, Université catholique de Louvain, 1200 Brussels, Belgium.

Vincent Stroobant (V)

Ludwig Institute for Cancer Research, 1200 Brussels, Belgium.
de Duve Institute, Université catholique de Louvain, 1200 Brussels, Belgium.

Delia Hoffmann (D)

Ludwig Institute for Cancer Research, 1200 Brussels, Belgium.
de Duve Institute, Université catholique de Louvain, 1200 Brussels, Belgium.

Mads Gyrd-Hansen (M)

Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom.

Luc Pilotte (L)

Ludwig Institute for Cancer Research, 1200 Brussels, Belgium.
de Duve Institute, Université catholique de Louvain, 1200 Brussels, Belgium.

Nathalie Vigneron (N)

Ludwig Institute for Cancer Research, 1200 Brussels, Belgium.
de Duve Institute, Université catholique de Louvain, 1200 Brussels, Belgium.

Etienne De Plaen (E)

Ludwig Institute for Cancer Research, 1200 Brussels, Belgium.
de Duve Institute, Université catholique de Louvain, 1200 Brussels, Belgium.

Benoit J Van den Eynde (BJ)

Ludwig Institute for Cancer Research, 1200 Brussels, Belgium; Benoit.Vandeneynde@bru.licr.org.
de Duve Institute, Université catholique de Louvain, 1200 Brussels, Belgium.
Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom.
Walloon Excellence in Life Sciences and Biotechnology, 1200 Brussels, Belgium.

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Classifications MeSH