Cargando…

ER chaperone GRP78/BiP translocates to the nucleus under stress and acts as a transcriptional regulator

Cancer cells are commonly subjected to endoplasmic reticulum (ER) stress. To gain survival advantage, cancer cells exploit the adaptive aspects of the unfolded protein response such as upregulation of the ER luminal chaperone GRP78. The finding that when overexpressed, GRP78 can escape to other cell...

Descripción completa

Detalles Bibliográficos
Autores principales:	Liu, Ze, Liu, Guanlin, Ha, Dat P., Wang, Justin, Xiong, Min, Lee, Amy S.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	National Academy of Sciences 2023
Materias:	Biological Sciences
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10400976/ https://www.ncbi.nlm.nih.gov/pubmed/37487081 http://dx.doi.org/10.1073/pnas.2303448120

Ejemplares similares

The stress-inducible ER chaperone GRP78/BiP is upregulated during SARS-CoV-2 infection and acts as a pro-viral protein
por: Shin, Woo-Jin, et al.
Publicado: (2022)

A novel pathogenic role of the ER chaperone GRP78/BiP in rheumatoid arthritis
por: Yoo, Seung-Ah, et al.
Publicado: (2012)

The Molecular Chaperone GRP78/BiP in the Development of Chemoresistance: Mechanism and Possible Treatment
por: Roller, Corinna, et al.
Publicado: (2013)

Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast
Publicado: (1990)

The Endoplasmic Reticulum Chaperone GRP78/BiP Modulates Prion Propagation in vitro and in vivo
por: Park, Kyung-Won, et al.
Publicado: (2017)

BiP chaperones ER entry
por: LeBrasseur, Nicole
Publicado: (2005)

Reply to: The stress-inducible ER chaperone GRP78/BiP is upregulated during SARS-CoV-2 infection and acts as a pro-viral protein
por: Shaban, Mohammed Samer, et al.
Publicado: (2022)

The molecular chaperone BiP (GRP 78) inhibits the differentiation of normal human monocytes into immature dendritic cells
por: Vittecoq, O, et al.
Publicado: (2003)

Endoplasmic reticulum chaperone BiP/GRP78 knockdown leads to autophagy and cell death of arginine vasopressin neurons in mice
por: Kawaguchi, Yohei, et al.
Publicado: (2020)

Cab45S inhibits the ER stress-induced IRE1-JNK pathway and apoptosis via GRP78/BiP
por: Chen, L, et al.
Publicado: (2014)

Data on the optimizations of expression and purification of human BiP/GRP78 protein in Escherichia coli
por: Yang, Jiao, et al.
Publicado: (2016)

HKH40A downregulates GRP78/BiP expression in cancer cells
por: Kosakowska-Cholody, T, et al.
Publicado: (2014)

Lysozyme Mutants Accumulate in Cells while Associated at their N-terminal Alpha-domain with the Endoplasmic Reticulum Chaperone GRP78/BiP
por: Kamada, Yoshiki, et al.
Publicado: (2016)

The endoplasmic reticulum chaperone BiP is a closure-accelerating cochaperone of Grp94
por: Huang, Bin, et al.
Publicado: (2022)

Endoplasmic Reticulum Stress-Associated Chaperones, Bip/GRP78 and Calnexin are Overexpressed in Keratocystic Odontogenic Tumours
por: Pavli, Maria, et al.
Publicado: (2014)

Mild Endoplasmic Reticulum Stress Promotes Retinal Neovascularization via Induction of BiP/GRP78
por: Nakamura, Shinsuke, et al.
Publicado: (2013)

GRP78/BiP determines senescence evasion cell fate after cisplatin-based chemotherapy
por: Ei, Zin Zin, et al.
Publicado: (2021)

Generation of human ER chaperone BiP in yeast Saccharomyces cerevisiae
por: Čiplys, Evaldas, et al.
Publicado: (2014)

Expression and clinical significance of Glucose Regulated Proteins GRP78 (BiP) and GRP94 (GP96) in human adenocarcinomas of the esophagus
por: Langer, Rupert, et al.
Publicado: (2008)

Vulnerability of The Male Reproductive System to SARS-CoV-2 Invasion: Potential Role for The Endoplasmic Reticulum Chaperone Grp78/HSPA5/BiP
por: Sadeghi, Niloofar, et al.
Publicado: (2022)

Essential role of the unfolded protein response regulator GRP78/BiP in protection from neuronal apoptosis
por: Wang, Miao, et al.
Publicado: (2009)

GRP78/BiP/HSPA5/Dna K is a Universal Therapeutic Target for Human Disease
por: Booth, Laurence, et al.
Publicado: (2015)

Selective Inactivation of Intracellular BiP/GRP78 Attenuates Endothelial Inflammation and Permeability in Acute Lung Injury
por: Leonard, Antony, et al.
Publicado: (2019)

New progresses on cell surface protein HSPA5/BiP/GRP78 in cancers and COVID-19
por: Li, Ting, et al.
Publicado: (2023)

The stress-inducible molecular chaperone GRP78 as potential therapeutic target for coronavirus infection
por: Ha, Dat P., et al.
Publicado: (2020)

The chaperone GRP78 is a host auxiliary factor for SARS-CoV-2 and GRP78 depleting antibody blocks viral entry and infection
por: Carlos, Anthony J., et al.
Publicado: (2021)

BiP/GRP78 Mediates ERAD Targeting of Proteins Produced by Membrane-Bound Ribosomes Stalled at the STOP-Codon
por: Cesaratto, Francesca, et al.
Publicado: (2019)

The Clinicopathological Significance of BiP/GRP-78 in Breast Cancer: A Meta-Analysis of Public Datasets and Immunohistochemical Detection
por: Direito, Inês, et al.
Publicado: (2022)

Direct interaction of the molecular chaperone GRP78/BiP with the Newcastle disease virus hemagglutinin-neuraminidase protein plays a vital role in viral attachment to and infection of culture cells
por: Han, Chenxin, et al.
Publicado: (2023)

FICD acts bi-functionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP
por: Preissler, Steffen, et al.
Publicado: (2016)

Suppression of ER-stress induction of GRP78 as an anti-neoplastic mechanism of the cardiac glycoside Lanatoside C in pancreatic cancer: Lanatoside C suppresses GRP78 stress induction
por: Ha, Dat P., et al.
Publicado: (2021)

It's a chaperone … it's a gatekeeper … it's BiP
por: Dove, Alan W.
Publicado: (2002)

Regulation of PERK Signaling and Leukemic Cell Survival by a Novel Cytosolic Isoform of the UPR Regulator GRP78/BiP
por: Ni, Min, et al.
Publicado: (2009)

Enterovirus 71 induces dsRNA/PKR-dependent cytoplasmic redistribution of GRP78/BiP to promote viral replication
por: Jheng, Jia-Rong, et al.
Publicado: (2016)

The Circulating GRP78/BiP Is a Marker of Metabolic Diseases and Atherosclerosis: Bringing Endoplasmic Reticulum Stress into the Clinical Scenario
por: Girona, Josefa, et al.
Publicado: (2019)

A Peptidic Unconjugated GRP78/BiP Ligand Modulates the Unfolded Protein Response and Induces Prostate Cancer Cell Death
por: Maddalo, Danilo, et al.
Publicado: (2012)

Androgen receptor inclusions acquire GRP78/BiP to ameliorate androgen-induced protein misfolding stress in embryonic stem cells
por: Yang, Y-C, et al.
Publicado: (2013)

Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum
Publicado: (1995)

UPR proteins IRE1 and PERK switch BiP from chaperone to ER stress sensor
por: Kopp, Megan C, et al.
Publicado: (2019)

XBP1-Mediated BiP/GRP78 Upregulation Copes with Oxidative Stress in Mosquito Cells during Dengue 2 Virus Infection
por: Chen, Tien-Huang, et al.
Publicado: (2017)

Cannot write session to /tmp/vufind_sessions/sess_ue3mu6q6uav5685qpv4uiu5l0i