title: A novel ER stress-independent function of the UPR in angiogenesis.
abstract: Tumors rely on the unfolded protein response (UPR) and angiogenesis to survive the metabolic stress of hypoxia. Karali et al. (2014) revealed that VEGF signaling engages UPR sensors in an unconventional manner that is independent of endoplasmic reticulum (ER) stress, mediated by mTOR signaling to promote endothelial cell survival and angiogenesis.
authors.affiliation: Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, Chile; Program of Cellular and Molecular Biology, Center for Molecular Studies of the Cell, Institute of Biomedical Sciences, University of Chile, Santiago, Chile.
authors.forename: Hery
authors.initials: H
authors.lastname: Urra
authors.affiliation: Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, Chile; Program of Cellular and Molecular Biology, Center for Molecular Studies of the Cell, Institute of Biomedical Sciences, University of Chile, Santiago, Chile; Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115, USA; Neurounion Biomedical Foundation, Santiago, Chile. Electronic address: chetz@med.uchile.cl.
authors.forename: Claudio
authors.initials: C
authors.lastname: Hetz
mesh_terms: D051702:Activating Transcription Factor 6 / Q000378:metabolism*; D000818:Animals; D059865:Endoplasmic Reticulum Stress; D042783:Endothelial Cells / Q000502:physiology*; D006801:Humans; D008297:Male; D009389:Neovascularization, Pathologic; D056811:Unfolded Protein Response; D042461:Vascular Endothelial Growth Factor A / Q000378:metabolism*; D019892:eIF-2 Kinase / Q000378:metabolism*
chemical_list: D051702:Activating Transcription Factor 6; D042461:Vascular Endothelial Growth Factor A; D019892:eIF-2 Kinase