Recent advances in signal integration mechanisms in the unfolded protein response

G Elif Karagöz; Tomás Aragón; Diego Acosta-Alvear

doi:10.12688/f1000research.19848.1

Recent advances in signal integration mechanisms in the unfolded protein response

F1000Res. 2019 Nov 1:8:F1000 Faculty Rev-1840. doi: 10.12688/f1000research.19848.1. eCollection 2019.

Authors

G Elif Karagöz¹, Tomás Aragón², Diego Acosta-Alvear³

Affiliations

¹ Max Perutz Labs Vienna, Medical University of Vienna, Vienna, Austria.
² Department of Gene Therapy and Regulation of Gene Expression, University of Navarra, Pamplona, Spain.
³ Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, Santa Barbara, Santa Barbara, CA, USA.

Abstract

Since its discovery more than 25 years ago, great progress has been made in our understanding of the unfolded protein response (UPR), a homeostatic mechanism that adjusts endoplasmic reticulum (ER) function to satisfy the physiological demands of the cell. However, if ER homeostasis is unattainable, the UPR switches to drive cell death to remove defective cells in an effort to protect the health of the organism. This functional dichotomy places the UPR at the crossroads of the adaptation versus apoptosis decision. Here, we focus on new developments in UPR signaling mechanisms, in the interconnectivity among the signaling pathways that make up the UPR in higher eukaryotes, and in the coordination between the UPR and other fundamental cellular processes.

Keywords: ER stress; signal transduction pathway interconnectivity; unfolded protein response.

Publication types

Review

MeSH terms

Apoptosis
Endoplasmic Reticulum
Endoplasmic Reticulum Stress*
Signal Transduction*
Unfolded Protein Response* / physiology

Grants and funding

The author(s) declared that no grants were involved in supporting this work.