Ubiquitylation of the ER-Shaping Protein Lunapark via the CRL3

Adaptor Proteins, Signal Transducing / metabolism Animals Animals, Genetically Modified Cell Line, Tumor Cullin Proteins / metabolism Endoplasmic Reticulum / metabolism HEK293 Cells Humans Mechanistic Target of Rapamycin Complex 1 / metabolism Membrane Proteins / metabolism Ubiquitin-Protein Ligases / metabolism Ubiquitination Zebrafish
ER three-way junction Lunapark cullin-RING ligases endoplasmic reticulum lysosome mTORC1 ubiquitin

Journal

Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691

Informations de publication

Date de publication:
19 05 2020
Historique:
received: 12 03 2019
revised: 16 01 2020
accepted: 28 04 2020
entrez: 21 5 2020
pubmed: 21 5 2020
medline: 22 5 2021
Statut: ppublish

Résumé

Cullin-RING ligases (CRLs) control key cellular processes by promoting ubiquitylation of a multitude of soluble cytosolic and nuclear proteins. Subsets of CRL complexes are recruited and activated locally at cellular membranes; however, few CRL functions and substrates at these distinct cellular compartments are known. Here, we use a proteomic screen to identify proteins that are ubiquitylated at cellular membranes and found that Lunapark, an endoplasmic reticulum (ER)-shaping protein localized to ER three-way junctions, is ubiquitylated by the CRL3

Identifiants

DOI: 10.1016/j.celrep.2020.107664 PMID: 32433973
pubmed: 32433973
pii: S2211-1247(20)30617-3
doi: 10.1016/j.celrep.2020.107664
pii:
doi:

Substances chimiques

Adaptor Proteins, Signal Transducing 0
Cullin Proteins 0
KLHL12 protein, human 0
LNPK protein, human 0
Membrane Proteins 0
Ubiquitin-Protein Ligases EC 2.3.2.27
Mechanistic Target of Rapamycin Complex 1 EC 2.7.11.1

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

107664

Informations de copyright

Copyright © 2020 The Author(s). Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Interests The authors declare no competing interests.

Auteurs

Laurensia Yuniati (L)

Hubrecht Institute-KNAW and University Medical Center Utrecht, 3584 CT Utrecht, the Netherlands.

Angela Lauriola (A)

Department of Biotechnology, University of Verona, 37134 Verona, Italy.

Manouk Gerritsen (M)

Hubrecht Institute-KNAW and University Medical Center Utrecht, 3584 CT Utrecht, the Netherlands.

Susana Abreu (S)

Hubrecht Institute-KNAW and University Medical Center Utrecht, 3584 CT Utrecht, the Netherlands.

Eric Ni (E)

Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, NYU Langone Health, New York, NY 10016, USA.

Chiara Tesoriero (C)

Department of Biotechnology, University of Verona, 37134 Verona, Italy.

Jacob O Onireti (JO)

Department of Biotechnology, University of Verona, 37134 Verona, Italy.

Teck Yew Low (TY)

UKM Medical Molecular Biology Institute (UMBI), Universiti Kebangsaan Malaysia, 56000 Kuala Lumpur, Malaysia.

Albert J R Heck (AJR)

Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 CH Utrecht, the Netherlands; The Netherlands Proteomics Center, 3584 CH Utrecht, the Netherlands.

Andrea Vettori (A)

Department of Biotechnology, University of Verona, 37134 Verona, Italy.

Timothy Cardozo (T)

Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, NYU Langone Health, New York, NY 10016, USA.

Daniele Guardavaccaro (D)

Hubrecht Institute-KNAW and University Medical Center Utrecht, 3584 CT Utrecht, the Netherlands; Department of Biotechnology, University of Verona, 37134 Verona, Italy. Electronic address: daniele.guardavaccaro@univr.it.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines adaptatrices de la transduction du signal › Ubiquitylation of the ER-Shaping Protein...
questionsmedicales.fr › Eucaryotes › Animaux › Ubiquitylation of the ER-Shaping Protein...
questionsmedicales.fr › Stades d'organismes › Organismes génétiquement modifiés › Animal génétiquement modifié › Ubiquitylation of the ER-Shaping Protein...
questionsmedicales.fr › Cellules › Cellules cultivées › Cellules cancéreuses en culture › Lignée cellulaire tumorale › Ubiquitylation of the ER-Shaping Protein...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cycle cellulaire › Cullines › Ubiquitylation of the ER-Shaping Protein...
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Réticulum endoplasmique › Ubiquitylation of the ER-Shaping Protein...
questionsmedicales.fr › Cellules › Cellules épithéliales › Cellules HEK293 › Ubiquitylation of the ER-Shaping Protein...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Ubiquitylation of the ER-Shaping Protein...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › Sérine-thréonine kinases TOR › Complexe-1 cible mécanistique de la rapamycine › Ubiquitylation of the ER-Shaping Protein...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Ubiquitylation of the ER-Shaping Protein...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Ligases › Ubiquitin-protein ligase complexes › Ubiquitin-protein ligases › Ubiquitylation of the ER-Shaping Protein...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Modification traductionnelle des protéines › Maturation post-traductionnelle des protéines › Ubiquitination › Ubiquitylation of the ER-Shaping Protein...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Poissons › Cypriniformes › Cyprinidae › Danio zébré › Ubiquitylation of the ER-Shaping Protein...