2. Academic Validation
  3. Multivesicular body formation enhancement and exosome release during endoplasmic reticulum stress

Multivesicular body formation enhancement and exosome release during endoplasmic reticulum stress

  • Biochem Biophys Res Commun. 2016 Nov 11;480(2):166-172. doi: 10.1016/j.bbrc.2016.10.019.
Soshi Kanemoto 1,  Ryota Nitani 2,  Tatsuhiko Murakami 2,  Masayuki Kaneko 2,  Rie Asada 2,  Koji Matsuhisa 2,  Atsushi Saito 2,  Kazunori Imaizumi 3
Affiliations

Affiliations

  • 1 Department of Biochemistry, Institute of Biomedical and Health Sciences, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima, 734-8553, Japan. Electronic address: soshikanemoto@hiroshima-u.ac.jp.
  • 2 Department of Biochemistry, Institute of Biomedical and Health Sciences, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima, 734-8553, Japan.
  • 3 Department of Biochemistry, Institute of Biomedical and Health Sciences, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima, 734-8553, Japan. Electronic address: imaizumi@hiroshima-u.ac.jp.
PMID: 27725157 DOI: 10.1016/j.bbrc.2016.10.019
Abstract

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.

Keywords

Endoplasmic reticulum; Exosome; IRE1; Multivesicular body; PERK.

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