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Title: A DERL3-associated defect in the degradation of SLC2A1 mediates the Warburg effect
Author: López Serra, Paula
Marcilla, Miguel
Villanueva Garatachea, Alberto
Ramos Fernandez, Antonio
Palau, Anna
Leal, Lucía
Wahi, Jessica E.
Setién, Fernando
Szczesna, Karolina
Moutinho, Cátia
Martínez Cardús, Anna
Heyn, Holger
Sandoval, Juan
Puertas, Sara
Vidal-Bel, August
Sanjuan, Xavier
Martínez Balibrea, Eva
Viñals Canals, Francesc
Perales Losa, Carlos
Bramsem, Jesper B.
Ørntoft, Torben F.
Andersen, Claus L.
Tabernero Caturla, Josep
McDermott, Ultan
Boxer, Matthew B.
Vander Heiden, Matthew G.
Albar, Juan Pablo
Esteller, Manel
Keywords: Cèl·lules canceroses
Cancer cells
Issue Date: 3-Apr-2014
Publisher: Nature Publishing Group
Abstract: Cancer cells possess aberrant proteomes that can arise by the disruption of genes involved in physiological protein degradation. Here we demonstrate the presence of promoter CpG island hypermethylation-linked inactivation of DERL3 (Derlin-3), a key gene in the endoplasmic reticulum-associated protein degradation pathway, in human tumours. The restoration of in vitro and in vivo DERL3 activity highlights the tumour suppressor features of the gene. Using the stable isotopic labelling of amino acids in cell culture workflow for differential proteome analysis, we identify SLC2A1 (glucose transporter 1, GLUT1) as a downstream target of DERL3. Most importantly, SLC2A1 overexpression mediated by DERL3 epigenetic loss contributes to the Warburg effect in the studied cells and pinpoints a subset of human tumours with greater vulnerability to drugs targeting glycolysis.
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It is part of: Nature Communications, 2014, vol. 5
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ISSN: 2041-1723
Appears in Collections:Articles publicats en revistes (Patologia i Terapèutica Experimental)
Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL))
Articles publicats en revistes (Ciències Fisiològiques)

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