Abstract
Quality control systems in the endoplasmic reticulum (ER) mediated by unfolded protein response (UPR) and endoplasmic reticulum associated degradation (ERAD) ensure cellular function and organismal survival. Recent studies have suggested that ER quality-control systems in cancer cells may serve as a double-edged sword that aids progression as well as prevention of tumor growth in a context-dependent manner. Here we review recent advances in our understanding of the complex relationship between ER proteostasis and cancer pathology, with a focus on the two most conserved ER quality-control mechanisms--the IRE1α-XBP1 pathway of the UPR and SEL1L-HRD1 complex of the ERAD.
Keywords:
ERAD; IRE1α-XBP1; Protein folding; SEL1L–HRD1; UPR.
Copyright © 2015 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Cell Survival
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DNA-Binding Proteins / metabolism
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Endoplasmic Reticulum / metabolism*
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Endoplasmic Reticulum-Associated Degradation
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Endoribonucleases / metabolism
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Gene Expression Regulation, Neoplastic
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Homeostasis
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Humans
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Mice
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Neoplasms / genetics*
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Neoplasms / metabolism*
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Neoplasms / therapy*
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Protein Binding
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Protein Serine-Threonine Kinases / metabolism
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Proteins / metabolism
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Regulatory Factor X Transcription Factors
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Signal Transduction
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Transcription Factors / metabolism
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Ubiquitin-Protein Ligases / metabolism
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Unfolded Protein Response*
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X-Box Binding Protein 1
Substances
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DNA-Binding Proteins
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Proteins
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Regulatory Factor X Transcription Factors
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SEL1L protein, human
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Transcription Factors
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X-Box Binding Protein 1
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XBP1 protein, human
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Xbp1 protein, mouse
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SYVN1 protein, human
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Ubiquitin-Protein Ligases
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ERN1 protein, human
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Protein Serine-Threonine Kinases
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Endoribonucleases