Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 480, Issue 2, Pages 166-172Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2016.10.019
Keywords
Endoplasmic reticulum; Multivesicular body; Exosome; IRE1; PERK
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Funding
- Japan Society for the Promotion of Science KAKENHI [JP15K20001]
- Takeda Science Foundation
- Terumo Foundation for Life Sciences and Arts
- Mitsui Sumitomo Insurance Welfare Foundation
- Grants-in-Aid for Scientific Research [15K21706, 15K19516] Funding Source: KAKEN
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The endoplasmic reticulum (ER) plays a pivotal role in maintaining cellular homeostasis. However, numerous environmental and genetic factors give rise to ER stress by inducing an accumulation of unfolded proteins. Under ER stress conditions, cells initiate the unfolded protein response (UPR). Here, we demonstrate a novel aspect of the UPR by electron microscopy and immunostaining analyses, whereby multivesicular body (MVB) formation was enhanced after ER stress. This MVB formation was influenced by inhibition of ER stress transducers inositol required enzyme 1 (IRE1) and PKR-like ER kinase (PERK). Furthermore, exosome release was also increased during ER stress. However, in IRE1 or PERK deficient cells, exosome release was not upregulated, indicating that IRE1- and PERK-mediated pathways are involved in ER stress-dependent exosome release. (C) 2016 Elsevier Inc. All rights reserved.
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