TMEM2 Modulates ER Stress in a Non-canonical Manner

Renata L S Goncalves; Gökhan S Hotamisligil

doi:10.1016/j.cmet.2019.11.008

TMEM2 Modulates ER Stress in a Non-canonical Manner

Cell Metab. 2019 Dec 3;30(6):999-1001. doi: 10.1016/j.cmet.2019.11.008.

Authors

Renata L S Goncalves¹, Gökhan S Hotamisligil²

Affiliations

¹ Sabri Ülker Center, Department of Molecular Metabolism and Broad Institute of Harvard-MIT, Harvard T.H. Chan School of Public Health, Boston, MA, USA. Electronic address: rgoncal@hsph.harvard.edu.
² Sabri Ülker Center, Department of Molecular Metabolism and Broad Institute of Harvard-MIT, Harvard T.H. Chan School of Public Health, Boston, MA, USA. Electronic address: ghotamis@hsph.harvard.edu.

PMID: 31801059
DOI: 10.1016/j.cmet.2019.11.008

Abstract

Cells utilize multiple mechanisms to support endoplasmic reticulum (ER) function. The unfolded protein response, UPR^ER, is engaged during proteotoxic challenges to either mitigate ER stress or promote apoptosis. In a CRISPR-based genetic screen, Schinzel et al. (2019) identified TMEM2 as a mediator of ER stress tolerance independent of the individual branches of the canonical UPR^ER and linked this path to nematode longevity.

Publication types

Research Support, N.I.H., Extramural
Comment

MeSH terms

Apoptosis
Endoplasmic Reticulum
Endoplasmic Reticulum Stress
Homeostasis
Hyaluronoglucosaminidase*
Longevity*
Signal Transduction
Unfolded Protein Response

Substances

Hyaluronoglucosaminidase