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

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 pr...

Full description

Saved in:
Bibliographic Details
Published inTrends in cell biology Vol. 27; no. 10; pp. 699 - 700
Main Authors Aragón, Tomás, van Anken, Eelco
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.10.2017
Elsevier BV
Subjects
Animals
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Endoplasmic Reticulum Stress - physiology
Endoribonucleases - metabolism
Homeostasis
Humans
Membrane Glycoproteins - metabolism
Membrane Lipids - metabolism
Protein Binding - physiology
Protein folding
Protein-Serine-Threonine Kinases - metabolism
Proteostasis - physiology
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
Signal Transduction - physiology
Studies
Unfolded Protein Response - physiology
Yeast
Online AccessGet full text

Cover

More Information
Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0962-8924
1879-3088
DOI:10.1016/j.tcb.2017.08.010