A novel ER stress-independent function of the UPR in angiogenesis

Hery Urra; Claudio Hetz

doi:10.1016/j.molcel.2014.05.013

A novel ER stress-independent function of the UPR in angiogenesis

Mol Cell. 2014 May 22;54(4):542-4. doi: 10.1016/j.molcel.2014.05.013.

Authors

Hery Urra¹, Claudio Hetz²

Affiliations

¹ 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.
² 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.

PMID: 24856218
DOI: 10.1016/j.molcel.2014.05.013

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.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Activating Transcription Factor 6 / metabolism*
Animals
Endoplasmic Reticulum Stress*
Endothelial Cells / physiology*
Humans
Male
Neovascularization, Pathologic*
Unfolded Protein Response*
Vascular Endothelial Growth Factor A / metabolism*
eIF-2 Kinase / metabolism*

Substances

Activating Transcription Factor 6
Vascular Endothelial Growth Factor A
eIF-2 Kinase