PHD1 controls muscle mTORC1 in a hydroxylation-independent manner by stabilizing leucyl tRNA synthetase

mTORC1 is an important regulator of muscle mass. Here, the authors show that the PHD1 controls muscle mass in a hydroxylation-independent manner. PHD1 prevents the degradation of leucine sensor LRS during oxygen and amino acid depletion to ensure effective mTORC1 activation in response to leucine.

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Autores principales: Gommaar D’Hulst, Inés Soro-Arnaiz, Evi Masschelein, Koen Veys, Gillian Fitzgerald, Benoit Smeuninx, Sunghoon Kim, Louise Deldicque, Bert Blaauw, Peter Carmeliet, Leigh Breen, Peppi Koivunen, Shi-Min Zhao, Katrien De Bock
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Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/57ce964136154da49cd0e8f1b72242c1
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spelling oai:doaj.org-article:57ce964136154da49cd0e8f1b72242c12021-12-02T16:49:46ZPHD1 controls muscle mTORC1 in a hydroxylation-independent manner by stabilizing leucyl tRNA synthetase10.1038/s41467-019-13889-62041-1723https://doaj.org/article/57ce964136154da49cd0e8f1b72242c12020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13889-6https://doaj.org/toc/2041-1723mTORC1 is an important regulator of muscle mass. Here, the authors show that the PHD1 controls muscle mass in a hydroxylation-independent manner. PHD1 prevents the degradation of leucine sensor LRS during oxygen and amino acid depletion to ensure effective mTORC1 activation in response to leucine.Gommaar D’HulstInés Soro-ArnaizEvi MasscheleinKoen VeysGillian FitzgeraldBenoit SmeuninxSunghoon KimLouise DeldicqueBert BlaauwPeter CarmelietLeigh BreenPeppi KoivunenShi-Min ZhaoKatrien De BockNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Gommaar D’Hulst
Inés Soro-Arnaiz
Evi Masschelein
Koen Veys
Gillian Fitzgerald
Benoit Smeuninx
Sunghoon Kim
Louise Deldicque
Bert Blaauw
Peter Carmeliet
Leigh Breen
Peppi Koivunen
Shi-Min Zhao
Katrien De Bock
PHD1 controls muscle mTORC1 in a hydroxylation-independent manner by stabilizing leucyl tRNA synthetase
description mTORC1 is an important regulator of muscle mass. Here, the authors show that the PHD1 controls muscle mass in a hydroxylation-independent manner. PHD1 prevents the degradation of leucine sensor LRS during oxygen and amino acid depletion to ensure effective mTORC1 activation in response to leucine.
format article
author Gommaar D’Hulst
Inés Soro-Arnaiz
Evi Masschelein
Koen Veys
Gillian Fitzgerald
Benoit Smeuninx
Sunghoon Kim
Louise Deldicque
Bert Blaauw
Peter Carmeliet
Leigh Breen
Peppi Koivunen
Shi-Min Zhao
Katrien De Bock
author_facet Gommaar D’Hulst
Inés Soro-Arnaiz
Evi Masschelein
Koen Veys
Gillian Fitzgerald
Benoit Smeuninx
Sunghoon Kim
Louise Deldicque
Bert Blaauw
Peter Carmeliet
Leigh Breen
Peppi Koivunen
Shi-Min Zhao
Katrien De Bock
author_sort Gommaar D’Hulst
title PHD1 controls muscle mTORC1 in a hydroxylation-independent manner by stabilizing leucyl tRNA synthetase
title_short PHD1 controls muscle mTORC1 in a hydroxylation-independent manner by stabilizing leucyl tRNA synthetase
title_full PHD1 controls muscle mTORC1 in a hydroxylation-independent manner by stabilizing leucyl tRNA synthetase
title_fullStr PHD1 controls muscle mTORC1 in a hydroxylation-independent manner by stabilizing leucyl tRNA synthetase
title_full_unstemmed PHD1 controls muscle mTORC1 in a hydroxylation-independent manner by stabilizing leucyl tRNA synthetase
title_sort phd1 controls muscle mtorc1 in a hydroxylation-independent manner by stabilizing leucyl trna synthetase
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/57ce964136154da49cd0e8f1b72242c1
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