TMEM2 Modulates ER Stress in a Non-canonical Manner

Cells utilize multiple mechanisms to support endoplasmic reticulum (ER) function. The unfolded protein response, UPRER, 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...

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Bibliographic Details
Published in:Cell metabolism 2019-12, Vol.30 (6), p.999-1001
Main Authors: Goncalves, Renata L.S., Hotamisligil, Gökhan S.
Format: Article
Language:English
Subjects:
Apoptosis
Endoplasmic Reticulum
Endoplasmic Reticulum Stress
Homeostasis
Hyaluronoglucosaminidase
Longevity
Signal Transduction
Unfolded Protein Response
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Summary:Cells utilize multiple mechanisms to support endoplasmic reticulum (ER) function. The unfolded protein response, UPRER, 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 UPRER and linked this path to nematode longevity. Cells utilize multiple mechanisms to support endoplasmic reticulum (ER) function. The unfolded protein response, UPRER, is engaged during proteotoxic challenges that either mitigate ER stress or promote apoptosis. In a CRISPR knockout screen, Schinzel et al. identified TMEM2 as a mediator of ER stress tolerance independent of the individual branches of the canonical UPRER and linked this path to nematode longevity.
ISSN:1550-4131
1932-7420
DOI:10.1016/j.cmet.2019.11.008