RNF26 and vimentin orchestrate ER stress recovery

P Strzyz - Nature Reviews Molecular Cell Biology, 2023 - nature.com
RNF26 and vimentin orchestrate ER stress recovery | Nature Reviews Molecular Cell Biology
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Vimentin intermediate filaments organize organellar architecture in response to ER stress

T Cremer, LM Voortman, E Bos, DM van Elsland… - bioRxiv, 2022 - biorxiv.org
Compartmentalization of organelles in space and time affects their functional state and
enables higher order regulation of essential cellular processes. How organellar residence is …

RNF26 binds perinuclear vimentin filaments to integrate ER and endolysosomal responses to proteotoxic stress

T Cremer, LM Voortman, E Bos, MLM Jongsma… - The EMBO …, 2023 - embopress.org
Proteotoxic stress causes profound endoplasmic reticulum (ER) membrane remodeling into
a perinuclear quality control compartment (ERQC) for the degradation of misfolded proteins …

[HTML][HTML] Calling RNF168 to action

S Nowsheen, Z Lou - Cell Stress, 2018 - ncbi.nlm.nih.gov
Genomic stress leads to various forms of DNA damage, of which DNA double strand breaks
(DSBs) are the most lethal. An army of signaling molecules is called to action as soon as …

IRE1α governs cytoskeleton remodelling and cell migration through a direct interaction with filamin A

H Urra, DR Henriquez, J Cánovas… - Nature cell …, 2018 - nature.com
Maintenance of endoplasmic reticulum (ER) proteostasis is controlled by a signalling
network known as the unfolded protein response (UPR). Here, we identified filamin A as a …

Transmembrane E3 ligase RNF183 mediates ER stress-induced apoptosis by degrading Bcl-xL

Y Wu, X Li, J Jia, Y Zhang, J Li, Z Zhu… - Proceedings of the …, 2018 - National Acad Sciences
The accumulation of misfolded proteins in the endoplasmic reticulum (ER) causes ER stress
and triggers the unfolded protein response (UPR). Failure to resolve ER stress leads to …

The ER structural protein Rtn4A stabilizes and enhances signaling through the receptor tyrosine kinase ErbB3

J Hatakeyama, JH Wald, H Rafidi, A Cuevas… - Science …, 2016 - science.org
ErbB3 and ErbB4 are receptor tyrosine kinases that are activated by the neuregulin (NRG)
family of growth factors. These receptors govern various developmental processes, and their …

PERK and filamin A in actin cytoskeleton remodeling at ER-plasma membrane contact sites

AR van Vliet, P Agostinis - Molecular & Cellular Oncology, 2017 - Taylor & Francis
The endoplasmic reticulum (ER) stress sensor protein kinase RNA-like endoplasmic
reticulum kinase (PERK) plays a major role during the unfolded protein response (UPR) …

[HTML][HTML] ER-trafficking triggers NRF1 ubiquitination to promote its proteolytic activation

C Chavarria, L Zaffalon, ST Ribeiro, M Op, M Quadroni… - Iscience, 2023 - cell.com
The transcription factor NRF1 resides in the endoplasmic reticulum (ER) and is constantly
transported to the cytosol for proteasomal degradation. However, when the proteasome is …

Control of nuclear envelope dynamics during acute ER stress by LINC complexes disassembly and selective, asymmetric autophagy of the outer nuclear membrane

MK Kucińska, M Molinari - Autophagy, 2024 - Taylor & Francis
The endoplasmic reticulum (ER) extends to the outer (ONM) and the inner (INM) nuclear
membrane forming the nuclear envelope (NE) that delimits the nucleoplasm containing the …