Results 91 to 100 of about 15,549 (206)

Ubiquitin and ubiquitin‐like modifications in the endoplasmic reticulum stress response

The FEBS Journal, EarlyView.
Endoplasmic reticulum (ER) stress activates various proteostasis control processes, including the unfolded protein response, ribosome‐associated quality control, and ER‐associated degradation. Ubiquitin and ubiquitin‐like modifications dynamically regulate these processes to determine cell fate, promoting adaptation or inducing cell death.
Tony Avril, Matthieu Le Gallo, Elodie Lafont   +2 more
wiley   +1 more source

Dual IRE1 targets: Determinants of the cell fate?

The FEBS Journal, EarlyView.
IRE1 is an ER stress sensor that restores protein homeostasis through two signaling activities: XBP1s, which upregulates its target gene expression or RIDD which downregulates its target transcripts. We recently identified Dual IRE1 Targets (DIT) which are modulated by both XBP1s and RIDD activities.
Eva Billat, Léane Legrand, Tony Avril, Elodie Lafont   +3 more
wiley   +1 more source

Sigma-1 receptor chaperone at the ER-mitochondrion interface mediates the mitochondrion-ER-nucleus signaling for cellular survival.

PLoS ONE, 2013
The membrane of the endoplasmic reticulum (ER) of a cell forms contacts directly with mitochondria whereby the contact is referred to as the mitochondrion-associated ER membrane or the MAM.
Tomohisa Mori, Teruo Hayashi, Eri Hayashi, Tsung-Ping Su   +3 more
doaj   +1 more source

NAA10 and BTRC drive CREBRF degradation in endoplasmic reticulum stress and renal tubular injury

Journal of Diabetes Investigation, EarlyView.
In diabetic kidney disease (DKD), the acetyltransferase NAA10 mediates the acetylation of CREBRF, promoting its recognition and binding by the E3 ubiquitin ligase BTRC, thereby enhancing the ubiquitination level of CREBRF and accelerating its degradation.
Sitian Fang, Jing Ning, Jinjing Huang, Yanxia Chen   +3 more
wiley   +1 more source

IRE1 directs proteasomal and lysosomal degradation of misfolded rhodopsin

Molecular Biology of the Cell, 2012
Endoplasmic reticulum (ER) is responsible for folding of secreted and membrane proteins in eukaryotic cells. Disruption of ER protein folding leads to ER stress. Chronic ER stress can cause cell death and is proposed to underlie the pathogenesis of many human diseases. Inositol-requiring enzyme 1 (IRE1) directs a key unfolded protein response signaling
Chiang, Wei-Chieh, Messah, Carissa, Lin, Jonathan H.   +2 more
openaire   +2 more sources

SIB1‐SEC23A undergo ER to chloroplast relocalization to mediate immunity in Arabidopsis thaliana

Journal of Integrative Plant Biology, EarlyView.
SEC23A mediates membrane trafficking between the endoplasmic reticulum (ER) and Golgi apparatus and interacts with the immunity protein SIGMA FACTOR‐BINDING PROTEIN1 in Arabidopsis. Under stress, both proteins relocate from the ER to chloroplasts, suppressing photosynthesis genes and enhancing defense genes.
Jialin Peng, Huan Zhong, Jianan Zhang, Hailei Zhang, Wuzhen Liu, Yonglun Zeng, Liwen Jiang, Yiji Xia   +7 more
wiley   +1 more source

IRE1 is a promising therapeutic target in pancreatic cancer

American Journal of Physiology-Cell Physiology
[Figure: see text]
Denise Lucas, Tamal Sarkar, Clara Y. Niemeyer, Julian C. Harnoss, Martin Schneider, Moritz J. Strowitzki, Jonathan M. Harnoss   +6 more
openaire   +2 more sources

Innovations in Obesity Treatment: Beyond Adipose Tissue Dysfunction

Obesity Reviews, EarlyView.
Obesity drives chronic inflammation, insulin resistance, type 2 diabetes, and cancer development through adipocyte dysfunction. Addressing this multisystemic disorder requires integrated strategies beyond diet and exercise, such as thermogenesis activation via menthol or capsinoids and appetite control through GLP‐1/GIP agonists and neuromodulation to ...
Jesica Martínez‐Godfrey, Irene Pomares‐Bri, Paula de Juan‐Maciá, Mariló Olivares‐Vicente, Enrique Barrajón‐Catalán, Vicente Micol, Enrique Roche, María Herranz‐López   +7 more
wiley   +1 more source

The Endoplasmic Reticulum Stress Sensor Inositol-Requiring Enzyme 1α Augments Bacterial Killing through Sustained Oxidant Production

mBio, 2015
Bacterial infection can trigger cellular stress programs, such as the unfolded protein response (UPR), which occurs when misfolded proteins accumulate within the endoplasmic reticulum (ER).
Basel H. Abuaita, Kristin M. Burkholder, Blaise R. Boles, Mary X. O’Riordan   +3 more
doaj   +1 more source

Unfolding Plant Defence: Endoplasmic Reticulum Stress Signalling at the Plant‐Pathogen Interface

Plant Biotechnology Journal, EarlyView.
ABSTRACT The endoplasmic reticulum (ER) stress response, a conserved proteostasis network, has emerged as a central hub that reprograms plant immunity during pathogen attack. This review synthesises how plants harness ER‐stress signalling to mount multilayered defences and how pathogens have evolved counterstrategies to subvert these pathways.
Zhe Meng, Shuqin Zheng, Federica Brandizzi, Yiran Liu, Chunlei Li, Congcong Ai, Yujiao Wang, Jiadong Qi, Xiuguo Zhang   +8 more
wiley   +1 more source