Loss of N-Glycanase 1 Alters Transcriptional and Translational Regulation in K562 Cell Lines.


Journal

G3 (Bethesda, Md.)
ISSN: 2160-1836
Titre abrégé: G3 (Bethesda)
Pays: England
ID NLM: 101566598

Informations de publication

Date de publication:
04 05 2020
Historique:
pubmed: 9 4 2020
medline: 22 6 2021
entrez: 9 4 2020
Statut: epublish

Résumé

N-Glycanase 1 (NGLY1) deficiency is an ultra-rare, complex and devastating neuromuscular disease. Patients display multi-organ symptoms including developmental delays, movement disorders, seizures, constipation and lack of tear production. NGLY1 is a deglycosylating protein involved in the degradation of misfolded proteins retrotranslocated from the endoplasmic reticulum (ER). NGLY1-deficient cells have been reported to exhibit decreased deglycosylation activity and an increased sensitivity to proteasome inhibitors. We show that the loss of NGLY1 causes substantial changes in the RNA and protein landscape of K562 cells and results in downregulation of proteasomal subunits, consistent with its processing of the transcription factor NFE2L1. We employed the CMap database to predict compounds that can modulate NGLY1 activity. Utilizing our robust K562 screening system, we demonstrate that the compound NVP-BEZ235 (Dactosilib) promotes degradation of NGLY1-dependent substrates, concurrent with increased autophagic flux, suggesting that stimulating autophagy may assist in clearing aberrant substrates during NGLY1 deficiency.

Identifiants

pubmed: 32265286
pii: g3.119.401031
doi: 10.1534/g3.119.401031
pmc: PMC7202010
doi:

Substances chimiques

Proteasome Endopeptidase Complex EC 3.4.25.1
NGLY1 protein, human EC 3.5.1.52
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase EC 3.5.1.52

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

1585-1597

Informations de copyright

Copyright © 2020 Mueller et al.

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Auteurs

William F Mueller (WF)

European Molecular Biology Labs, Genome Biology Unit, Heidelberg, Germany, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Petra Jakob (P)

European Molecular Biology Labs, Genome Biology Unit, Heidelberg, Germany, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Han Sun (H)

Stanford University, CA, 94305.

Sandra Clauder-Münster (S)

European Molecular Biology Labs, Genome Biology Unit, Heidelberg, Germany, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Sonja Ghidelli-Disse (S)

Cellzome GmbH, a GlaxoSmithKline Company, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Diana Ordonez (D)

European Molecular Biology Labs, Genome Biology Unit, Heidelberg, Germany, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Markus Boesche (M)

Cellzome GmbH, a GlaxoSmithKline Company, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Marcus Bantscheff (M)

Cellzome GmbH, a GlaxoSmithKline Company, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Paul Collier (P)

European Molecular Biology Labs, Genome Biology Unit, Heidelberg, Germany, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Bettina Haase (B)

European Molecular Biology Labs, Genome Biology Unit, Heidelberg, Germany, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Vladimir Benes (V)

European Molecular Biology Labs, Genome Biology Unit, Heidelberg, Germany, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Malte Paulsen (M)

European Molecular Biology Labs, Genome Biology Unit, Heidelberg, Germany, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Peter Sehr (P)

European Molecular Biology Labs, Genome Biology Unit, Heidelberg, Germany, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Joe Lewis (J)

European Molecular Biology Labs, Genome Biology Unit, Heidelberg, Germany, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Gerard Drewes (G)

Cellzome GmbH, a GlaxoSmithKline Company, Meyerhofstrasse 1, Heidelberg, Germany, 69117.

Lars M Steinmetz (LM)

European Molecular Biology Labs, Genome Biology Unit, Heidelberg, Germany, Meyerhofstrasse 1, Heidelberg, Germany, 69117 lars.steinmetz@embl.de.
Stanford University, CA, 94305.

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Classifications MeSH