The Ire1 Twist that Links Proteostatic with Lipostatic Control of the Endoplasmic Reticulum

Tomás Aragón; Eelco van Anken

doi:10.1016/j.tcb.2017.08.010

The Ire1 Twist that Links Proteostatic with Lipostatic Control of the Endoplasmic Reticulum

Trends Cell Biol. 2017 Oct;27(10):699-700. doi: 10.1016/j.tcb.2017.08.010. Epub 2017 Sep 5.

Authors

Tomás Aragón¹, Eelco van Anken²

Affiliations

¹ Department of Gene Therapy and Regulation, Center for Applied Medical Research, University of Navarra. 55 Pio XII St. 31008 Pamplona, Spain.
² Division of Genetics and Cell Biology, San Raffaele Scientific Institute, Ospedale San Raffaele, Via Olgettina 58, 20132, Milan, Italy. Electronic address: [email protected].

PMID: 28886896
DOI: 10.1016/j.tcb.2017.08.010

Abstract

The unfolded protein response (UPR) governs homeostasis of both luminal content and membrane of the endoplasmic reticulum (ER). In Molecular Cell, Halbleib et al. identified how a twist in the juxta-membrane amphipathic helix of the UPR transducer Ire1 in yeast is essential for responding to both proteostatic and lipostatic ER stress.

MeSH terms

Animals
Endoplasmic Reticulum / metabolism*
Endoplasmic Reticulum Stress / physiology
Endoribonucleases / metabolism
Humans
Membrane Glycoproteins / metabolism
Membrane Lipids / metabolism
Protein Binding / physiology
Protein Serine-Threonine Kinases / metabolism*
Proteostasis / physiology
Saccharomyces cerevisiae / metabolism
Saccharomyces cerevisiae Proteins / metabolism
Signal Transduction / physiology
Unfolded Protein Response / physiology

Substances

Membrane Glycoproteins
Membrane Lipids
Saccharomyces cerevisiae Proteins
Protein Serine-Threonine Kinases
Endoribonucleases