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

Piña, Francisco; Niwa, Maho

doi:10.7554/elife.06970

Cited by 26 publications

(34 citation statements)

References 69 publications

(96 reference statements)

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“…If true, the latter scenario would suggest that pnER-localized and cER-localized Kar2-sfGFP acquire different properties during ER stress. To test the first possibility, we examined the formation of CPY*-mRFP or GFP-CFTR protein aggregates in each ER subdomain during ER stress (Kakoi et al, 2013; Fu and Sztul, 2003; Pina and Niwa, 2015). CPY*-mRFP aggregates activate both the UPR and ERSU pathways, whereas GFP-CFTR aggregates do not (Pina and Niwa, 2015).…”

Section: Resultsmentioning

confidence: 99%

“…To test the first possibility, we examined the formation of CPY*-mRFP or GFP-CFTR protein aggregates in each ER subdomain during ER stress (Kakoi et al, 2013; Fu and Sztul, 2003; Pina and Niwa, 2015). CPY*-mRFP aggregates activate both the UPR and ERSU pathways, whereas GFP-CFTR aggregates do not (Pina and Niwa, 2015). This difference allows us to observe the cER and pnER localization pattern of aggregates that do or do not induce ER stress.…”

Section: Resultsmentioning

confidence: 99%

“…ER inheritance and ER aggregate formation was imaged and analyzed as described previously (Pina and Niwa, 2015; Babour et al, 2010). The graphs represent the mean ± SD of 3 experiments, each analyzing ≥200 cells for cER inheritance or ≥100 cells for aggregate formation.…”

Section: Methodsmentioning

confidence: 99%

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Reticulons Regulate the ER Inheritance Block during ER Stress

et al. 2016

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Segregation of functional organelles during the cell cycle is crucial to generate healthy daughter cells. In S. cerevisiae, ER stress causes an ER inheritance block to ensure cells inherit a functional ER. Here, we report that formation of tubular ER in the mother cell, the first step in ER inheritance, depends on functional symmetry between the cortical ER (cER) and perinuclear ER (pnER). ER stress induces functional asymmetry, blocking tubular ER formation and ER inheritance. Using fluorescence recovery after photobleaching, we show that the ER chaperone Kar2/BiP fused to GFP and an ER membrane reporter, Hmg1-GFP, behave differently in the cER and pnER. The functional asymmetry and tubular ER formation depend on Reticulons/Yop1, which maintain ER structure. Lunapark1 deletion in rtn1Δrtn2Δyop1Δ cells restores the pnER/cER functional asymmetry, tubular ER generation and ER inheritance blocks. Thus, Reticulon/Yop1-dependent changes in ER structure are linked to ER inheritance during the yeast cell cycle.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Reticulons Regulate the ER Inheritance Block during ER Stress

et al. 2016

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“…Increasing attention has been given to ER stress for the roles it plays in many diseases, including diabetes [87], cardiovascular diseases [88], cancer [89], inflammation [90] and neurodegeneration [91]. IRE1α is the most sensitive UPR branch in mammalian cells upon ER stress.…”

Section: Discussionmentioning

confidence: 99%

IRE1α Signaling Pathways Involved in Mammalian Cell Fate Determination

Zhang

et al. 2016

Cell Physiol Biochem

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A diverse array of cellular stresses can lead to accumulation of misfolded or unfolded proteins in endoplasmic reticulum (ER), which subsequently elicits ER stress. Inositol-requiring enzyme 1α (IRE1α) is the most sensitive of the three unfolded protein response (UPR) branches which are triggered to cope with ER stress in mammalian cells. IRE1α signaling is quite context-specific on account of many adaptor and modulator proteins that directly interact with it, including heat shock proteins (HSPs), RING finger protein 13 (RNF13), poly (ADP-ribose) polymerase 16 (PARP16), Bax/Bak, and Bax inhibitor-1 (BI-1). The activated IRE1α triggers different downstream pathways depending on the UPRosome formed by distinct modulator proteins. At the initial phase of ER stress, IRE1α-XBP1 axis functions as an adaptive response. While ER stress sustains or intensifies, signals shift to apoptotic responses. Furthermore, IRE1α signaling can be exploited to the development of a wide range of prevalent human diseases, with cancer the most characterized. Here we provide an overview of recent insights into the complex IRE1α signaling network which makes IRE1α an intriguing cell fate switch. Besides, the functional relevance is presented since IRE1α activation also participates in some other physiological processes beyond protein-folding status.

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“…Previously, we discovered a cell cycle checkpoint for ensuring that functional ER is transferred to the daughter cell during the cell cycle, which we termed the ER stress surveillance (ERSU) pathway (Babour et al, 2010;Pina et al, 2018;Pina et al, 2016;Pina and Niwa, 2015). If the accumulation of unfolded or misfolded proteins exceeds ER functional capacity, ER homeostasis is disrupted, leading to a condition known as ER stress.…”

Section: Introductionmentioning

confidence: 99%

Transfer of Septin Rings to Cytokinetic Remnants Directs Age-Sensitive ER stress Surveillance Cell Cycle Re-entry

Chao¹,

Piña²,

Onishi

et al. 2019

Preprint

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SUMMARYDuring cell division, cells must actively pass on organelles. Previously, we discovered the endoplasmic reticulum (ER) stress surveillance (ERSU) pathway that ensures the inheritance of functional ER. Activation of the ERSU causes the septin ring to mislocalize, which blocks ER inheritance and cytokinesis. Here, we found that the septin ring mislocalizes to previously utilized cell division sites called cytokinetic remnants (CRMs). The transfer of the septin ring to CRMs requires Nba1, a negative polarity component that normally prevents septin ring formation at CRMs. Furthermore, septin ring movement to CRMs relies on the ERSU component Slt2, which is recruited by binding Bem1. During ER stress, Bem1 also binds the GTP exchange factor Cdc24, without activating Cdc42, a GTPase that normally establishes polarized growth. Failure to translocate septin rings to CRMs delays the cell’s ability to re-enter cell division when ER homeostasis is re-established. Thus, ER stress considers the history of previous cell cycle for future cell cycle re-entry upon ER stress recovery.

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

Cited by 26 publications

References 69 publications

Reticulons Regulate the ER Inheritance Block during ER Stress

Reticulons Regulate the ER Inheritance Block during ER Stress

IRE1α Signaling Pathways Involved in Mammalian Cell Fate Determination

Transfer of Septin Rings to Cytokinetic Remnants Directs Age-Sensitive ER stress Surveillance Cell Cycle Re-entry

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