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Semin Cancer Biol. 2015 Aug;33:48-56. doi: 10.1016/j.semcancer.2015.04.010. Epub 2015 May 16.

Targeting the IRE1α-XBP1 branch of the unfolded protein response in human diseases.

Author information

1
Department of Radiation Oncology, Stanford University School of Medicine, Stanford, CA 94305, USA.
2
Department of Biological Sciences, University of California, San Diego, CA 92093, USA.
3
Department of Radiation Oncology, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: akoong@stanford.edu.

Abstract

Accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER) leads to ER stress, which is characteristic of cells with high level of secretory activity and implicated in a variety of disease conditions. In response to ER stress, the cell elicits an adaptive process called the unfolded protein response (UPR) to support cellular homeostasis and survival. However, prolonged and unsolvable ER stress also induces apoptosis. As the most conserved signaling branch of the UPR, the IRE1α-XBP1 pathway plays important roles in both physiological and pathological settings and its activity has profound effects on disease progression and prognosis. Recently, modulating this pathway with small molecule compounds has been demonstrated as a promising approach for disease therapy. In this review, we summarize a list of current investigational compounds targeting this pathway and their therapeutic features for treating human diseases.

KEYWORDS:

Compounds; Drug discovery; ER stress; Protein folding; Therapy

PMID:
25986851
PMCID:
PMC4523453
DOI:
10.1016/j.semcancer.2015.04.010
[Indexed for MEDLINE]
Free PMC Article
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