The ER Stress Surveillance (ERSU) pathway regulates daughter cell ER protein aggregate inheritance

ELife
Francisco J Piña, Maho Niwa

Abstract

Stress induced by cytoplasmic protein aggregates can have deleterious consequences for the cell, contributing to neurodegeneration and other diseases. Protein aggregates are also formed within the endoplasmic reticulum (ER), although the fate of ER protein aggregates, specifically during cell division, is not well understood. By simultaneous visualization of both the ER itself and ER protein aggregates, we found that ER protein aggregates that induce ER stress are retained in the mother cell by activation of the ER Stress Surveillance (ERSU) pathway, which prevents inheritance of stressed ER. In contrast, under conditions of normal ER inheritance, ER protein aggregates can enter the daughter cell. Thus, whereas cytoplasmic protein aggregates are retained in the mother cell to protect the functional capacity of daughter cells, the fate of ER protein aggregates is determined by whether or not they activate the ERSU pathway to impede transmission of the cortical ER during the cell cycle.

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Citations

Apr 28, 2016·Developmental Cell·Francisco Javier PiñaMaho Niwa
Feb 23, 2018·Microbial Biotechnology·Elisabet Navarro-TapiaRoberto Pérez-Torrado
Jan 11, 2018·The Journal of Cell Biology·Francisco PiñaMaho Niwa
Feb 9, 2018·Journal of Cell Science·Linhao RuanRong Li
Jul 1, 2020·Development·Bharath Sunchu, Clemens Cabernard
Jan 16, 2021·Molecular Biology of the Cell·Jesse T ChaoMaho Niwa
Aug 24, 2020·Biochimica Et Biophysica Acta. Molecular Cell Research·Maho Niwa

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Methods Mentioned

BETA
glycosylation
protein-folding
fluorescence recovery after photobleaching
fluorescence microscopy
PCR

Software Mentioned

softWoRx

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