Base de dados : MEDLINE
Pesquisa : G02.111.660.871.790.600.962 [Categoria DeCS]
Referências encontradas : 2641 [refinar]
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  1 / 2641 MEDLINE  
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[PMID]:28459443
[Au] Autor:Tavernier SJ; Osorio F; Vandersarren L; Vetters J; Vanlangenakker N; Van Isterdael G; Vergote K; De Rycke R; Parthoens E; van de Laar L; Iwawaki T; Del Valle JR; Hu CA; Lambrecht BN; Janssens S
[Ad] Endereço:Laboratory of Immunoregulation and Mucosal Immunology, VIB Center for Inflammation Research, 9052 Ghent, Belgium.
[Ti] Título:Regulated IRE1-dependent mRNA decay sets the threshold for dendritic cell survival.
[So] Source:Nat Cell Biol;19(6):698-710, 2017 Jun.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The IRE1-XBP1 signalling pathway is part of a cellular programme that protects against endoplasmic reticulum (ER) stress, but also controls development and survival of immune cells. Loss of XBP1 in splenic type 1 conventional dendritic cells (cDC1s) results in functional alterations without affecting cell survival. However, in mucosal cDC1s, loss of XBP1 impaired survival in a tissue-specific manner-while lung cDC1s die, intestinal cDC1s survive. This was not caused by differential activation of ER stress cell-death regulators CHOP or JNK. Rather, survival of intestinal cDC1s was associated with their ability to shut down protein synthesis through a protective integrated stress response and their marked increase in regulated IRE1-dependent messenger RNA decay. Furthermore, loss of IRE1 endonuclease on top of XBP1 led to cDC1 loss in the intestine. Thus, mucosal DCs differentially mount ATF4- and IRE1-dependent adaptive mechanisms to survive in the face of ER stress.
[Mh] Termos MeSH primário: Células Dendríticas/enzimologia
Mucosa Intestinal/enzimologia
Proteínas de Membrana/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Estabilidade de RNA
RNA Mensageiro/metabolismo
Mucosa Respiratória/enzimologia
[Mh] Termos MeSH secundário: Fator 4 Ativador da Transcrição/genética
Fator 4 Ativador da Transcrição/metabolismo
Animais
Apoptose
Sobrevivência Celular
Células Dendríticas/patologia
Estresse do Retículo Endoplasmático
Genótipo
Mucosa Intestinal/patologia
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Proteínas de Membrana/genética
Camundongos Transgênicos
Fenótipo
Biossíntese de Proteínas
Proteínas Serina-Treonina Quinases/genética
RNA Mensageiro/genética
Mucosa Respiratória/patologia
Transdução de Sinais
Fatores de Tempo
Fator de Transcrição CHOP/genética
Fator de Transcrição CHOP/metabolismo
Resposta a Proteínas não Dobradas
Proteína 1 de Ligação a X-Box/genética
Proteína 1 de Ligação a X-Box/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Atf4 protein, mouse); 0 (Ddit3 protein, mouse); 0 (Membrane Proteins); 0 (RNA, Messenger); 0 (X-Box Binding Protein 1); 0 (Xbp1 protein, mouse); 145891-90-3 (Activating Transcription Factor 4); 147336-12-7 (Transcription Factor CHOP); EC 2.7.1.- (Ern2 protein, mouse); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3518


  2 / 2641 MEDLINE  
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[PMID]:29324796
[Au] Autor:Li XM; Liu J; Pan FF; Shi DD; Wen ZG; Yang PL
[Ad] Endereço:Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, China.
[Ti] Título:Quercetin and aconitine synergistically induces the human cervical carcinoma HeLa cell apoptosis via endoplasmic reticulum (ER) stress pathway.
[So] Source:PLoS One;13(1):e0191062, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Up till now, studies have not been conducted on how the combination of Quercetin (Q), Aconitine (A) and apoptosis induction affects human cervical carcinoma HeLa cells. The result of our findings shows that the combination of Q and A (QA) is capable of synergistically inhibiting the proliferation of HeLa cells in a number of concentrations. QA synergistically inhibits the proliferation of MDR1 gene in the HeLa cells. It is concluded based on our result that QA induces apoptosis and ER stress just as QA-induced ER stress pathway may mediate apoptosis by upregulating mRNA expression levels of eIF2α, ATF4, IRE1, XBP1, ATF6, PERK and CHOP in the HeLa cells. The up-regulating of mRNA expression level of GRP78 and activation of UPR are a molecular basis of QA-induced ER stress.
[Mh] Termos MeSH primário: Aconitina/farmacologia
Estresse do Retículo Endoplasmático/efeitos dos fármacos
Quercetina/farmacologia
Neoplasias do Colo do Útero/patologia
[Mh] Termos MeSH secundário: Subfamília B de Transportador de Cassetes de Ligação de ATP/genética
Apoptose/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Proliferação Celular/genética
Feminino
Células HeLa
Seres Humanos
Marcação In Situ das Extremidades Cortadas
Espécies Reativas de Oxigênio/metabolismo
Resposta a Proteínas não Dobradas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ABCB1 protein, human); 0 (ATP Binding Cassette Transporter, Sub-Family B); 0 (Reactive Oxygen Species); 9IKM0I5T1E (Quercetin); X8YN71D5WC (Aconitine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191062


  3 / 2641 MEDLINE  
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[PMID]:29277614
[Au] Autor:Barnault R; Lahlali T; Plissonnier ML; Romero-López C; Laverdure N; Ducarouge B; Rivoire M; Mehlen P; Zoulim F; Parent R
[Ad] Endereço:INSERM U1052 & CNRS UMR5286, Cancer Research Centre of Lyon, Lyon, France; University of Lyon, Lyon, France; DevWeCan Laboratories of Excellence Network (Labex), Lyon, France. Electronic address: romain.barnault@inserm.fr.
[Ti] Título:Hepatocellular carcinoma-associated depletion of the netrin-1 receptor Uncoordinated Phenotype-5A (UNC5A) skews the hepatic unfolded protein response towards prosurvival outcomes.
[So] Source:Biochem Biophys Res Commun;495(4):2425-2431, 2018 01 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the liver, HBV and HCV infections, exposure to toxics, genetic and metabolic disorders may induce endoplasmic reticulum (ER) stress and the unfolding protein response (UPR). The UPR allows cells to reach ER homeostasis after lumen overload, but also fosters survival of damaged cells and therefore HCC onset. Dependence receptors such as UNC5A trigger apoptosis when unbound to their ligands. We have previously shown that the main dependence receptor ligand, netrin-1, could protect cells against UPR-induced apoptosis through sustained translation. In this study, we show that UNC5A is cumulatively downregulated by the UPR at the transcriptional level in vitro and at the translational level both in vitro and in vivo. We have found that the 5'-untranslated region of the UNC5A mRNA shares a certain homology degree with that of netrin-1, suggesting linked translational regulatory mechanisms, at least during the initial stages of the UPR. RNAi and forced expression studies identified UNC5A as a modulator of cell death in the context of the UPR. UNC5A decrease of association with polysomes and expression oriented cells towards UPR-associated hepatocytic survival. Such data indicate that cooperation between the UPR and UNC5A depletion as previously observed by ourselves in HCC patients samples may foster liver cancer development and growth.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/genética
Carcinoma Hepatocelular/patologia
Neoplasias Hepáticas/genética
Neoplasias Hepáticas/patologia
Netrina-1/genética
Receptores de Superfície Celular/genética
Resposta a Proteínas não Dobradas/genética
[Mh] Termos MeSH secundário: Apoptose/genética
Carcinogênese
Linhagem Celular Tumoral
Repressão Epigenética/genética
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Receptors, Cell Surface); 0 (UNC5A protein, human); 158651-98-0 (Netrin-1)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171227
[St] Status:MEDLINE


  4 / 2641 MEDLINE  
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[PMID]:29233873
[Au] Autor:Smith M; Wilkinson S
[Ad] Endereço:Edinburgh Cancer Research UK Centre, MRC Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh EH4 2XR, U.K. s.wilkinson@ed.ac.uk Matthew.Smith@igmm.ed.ac.uk.
[Ti] Título:ER homeostasis and autophagy.
[So] Source:Essays Biochem;61(6):625-635, 2017 12 12.
[Is] ISSN:1744-1358
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The endoplasmic reticulum (ER) is a key site for lipid biosynthesis and folding of nascent transmembrane and secretory proteins. These processes are maintained by careful homeostatic control of the environment within the ER lumen. Signalling sensors within the ER detect perturbations within the lumen (ER stress) and employ downstream signalling cascades that engage effector mechanisms to restore homeostasis. The most studied signalling mechanism that the ER employs is the unfolded protein response (UPR), which is known to increase a number of effector mechanisms, including autophagy. In this chapter, we will discuss the emerging role of autophagy as a UPR effector pathway. We will focus on the recently discovered selective autophagy pathway for ER, ER-phagy, with particular emphasis on the structure and function of known mammalian ER-phagy receptors, namely FAM134B, SEC62, RTN3 and CCPG1. Finally, we conclude with our view of where the future of this field can lead our understanding of the involvement of ER-phagy in ER homeostasis.
[Mh] Termos MeSH primário: Autofagia/fisiologia
Retículo Endoplasmático/metabolismo
[Mh] Termos MeSH secundário: Animais
Autofagia/genética
Estresse do Retículo Endoplasmático/genética
Estresse do Retículo Endoplasmático/fisiologia
Homeostase/genética
Homeostase/fisiologia
Seres Humanos
Resposta a Proteínas não Dobradas/genética
Resposta a Proteínas não Dobradas/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.1042/EBC20170092


  5 / 2641 MEDLINE  
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[PMID]:27778132
[Au] Autor:Karthikeyan B; Harini L; Krishnakumar V; Kannan VR; Sundar K; Kathiresan T
[Ad] Endereço:Department of Biotechnology, Kalasalingam University, Anand Nagar, Krishnankoil, Tamil Nadu, 626 126, India.
[Ti] Título:Insights on the involvement of (-)-epigallocatechin gallate in ER stress-mediated apoptosis in age-related macular degeneration.
[So] Source:Apoptosis;22(1):72-85, 2017 Jan.
[Is] ISSN:1573-675X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Endoplasmic reticulum (ER) stress-mediated apoptosis is a well-known factor in the pathogenesis of age-related macular degeneration (AMD). ER stress leads to accumulation of misfolded proteins, which in turn activates unfolded protein response (UPR) of the cell for its survival. The prolonged UPR of ER stress promotes cell death; however, the transition between adaptation and ER stress-induced apoptosis has not been clearly understood. Hence, the present study investigates the regulatory effect of (-)-epigallocatechin gallate (EGCG) on ER stress-induced by hydrogen peroxide (H O ) and disturbance of calcium homeostasis by thapsigargin (TG) in mouse retinal pigment epithelial (MRPE) cells. The oxidant molecules influenced MRPE cells showed an increased level of intracellular calcium [Ca ] in ER and transferred to mitochondria through ER-mitochondrial tether site then increased ROS production. EGCG restores [Ca ] homeostasis by decreasing ROS production through inhibition of prohibitin1 which regulate ER-mitochondrial tether site and inhibit apoptosis. Effect of EGCG on ER stress-mediated apoptosis was elucidated by exploring the UPR signalling pathways. EGCG downregulated GRP78, CHOP, PERK, ERO1α, IRE1α, cleaved PARP, cleaved caspase 3, caspase 12 and upregulated expression of calnexinin MRPE cells. In addition to this, inhibition of apoptosis by EGCG was also confirmed with expression of proteins Akt, PTEN and GSK3ß. MRPE cells with EGCG upregulates phosphorylation of Akt at ser473 and phospho ser380 of PTEN, but phosphorylation at ser9 of GSK3ß was inhibited. Further, constitutively active (myristoylated) CA-Akt transfected in MRPE cells had an increased Akt activity in EGCG influenced cells. These findings strongly suggest that antioxidant molecules inhibit cell death through the proper balancing of [Ca ] and ROS production in order to maintain UPR of ER in MRPE cells. Thus, modulation of UPR signalling may provide a potential target for the therapeutic approaches of AMD.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Catequina/análogos & derivados
Estresse do Retículo Endoplasmático/efeitos dos fármacos
Degeneração Macular/tratamento farmacológico
Resposta a Proteínas não Dobradas/genética
[Mh] Termos MeSH secundário: Animais
Antioxidantes/metabolismo
Cálcio/metabolismo
Sinalização do Cálcio/genética
Catequina/administração & dosagem
Estresse do Retículo Endoplasmático/genética
Seres Humanos
Peróxido de Hidrogênio/toxicidade
Degeneração Macular/genética
Camundongos
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/genética
Estresse Oxidativo/efeitos dos fármacos
Espécies Reativas de Oxigênio/metabolismo
Tapsigargina/administração & dosagem
Resposta a Proteínas não Dobradas/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Reactive Oxygen Species); 67526-95-8 (Thapsigargin); 8R1V1STN48 (Catechin); BBX060AN9V (Hydrogen Peroxide); BQM438CTEL (epigallocatechin gallate); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE
[do] DOI:10.1007/s10495-016-1318-2


  6 / 2641 MEDLINE  
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[PMID]:28741511
[Au] Autor:Urra H; Dufey E; Avril T; Chevet E; Hetz C
[Ad] Endereço:Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, Chile; Center for Geroscience, Brain Health and Metabolism, Santiago, Chile; Program of Cellular and Molecular Biology, Institute of Biomedical Sciences, University of Chile, Santiago, Chile.
[Ti] Título:Endoplasmic Reticulum Stress and the Hallmarks of Cancer.
[So] Source:Trends Cancer;2(5):252-262, 2016 May.
[Is] ISSN:2405-8025
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tumor cells are often exposed to intrinsic and external factors that alter protein homeostasis, thus producing endoplasmic reticulum (ER) stress. To cope with this, cells evoke an adaptive mechanism to restore ER proteostasis known as the unfolded protein response (UPR). The three main UPR signaling branches initiated by IRE1α, PERK, and ATF6 are crucial for tumor growth and aggressiveness as well as for microenvironment remodeling or resistance to treatment. We provide a comprehensive overview of the contribution of the UPR to cancer biology and the acquisition of malignant characteristics, thus highlighting novel aspects including inflammation, invasion and metastasis, genome instability, resistance to chemo/radiotherapy, and angiogenesis. The therapeutic potential of targeting ER stress signaling in cancer is also discussed.
[Mh] Termos MeSH primário: Estresse do Retículo Endoplasmático
Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Animais
Transformação Celular Neoplásica
Resistência a Medicamentos Antineoplásicos
Epigênese Genética
Instabilidade Genômica
Seres Humanos
Invasividade Neoplásica
Neoplasias/genética
Neoplasias/patologia
Neoplasias/terapia
Resposta a Proteínas não Dobradas
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


  7 / 2641 MEDLINE  
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[PMID]:28741509
[Au] Autor:Galmiche A; Sauzay C; Houessinon A; Chauffert B; Pluquet O
[Ad] Endereço:Service de Biochimie, Centre de Biologie Humaine (CBH), CHU Amiens Sud, France; EA4666, Université de Picardie Jules Verne (UPJV), Amiens, France. Electronic address: Galmiche.Antoine@chu-amiens.fr.
[Ti] Título:Probing Tumour Proteostasis and the UPR with Serum Markers.
[So] Source:Trends Cancer;2(5):219-221, 2016 May.
[Is] ISSN:2405-8025
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tumour proteostasis and the unfolded protein response (UPR) are emerging drivers of tumour progression and important determinants of clinical efficacy of cancer therapy. Recent findings indicate that they also regulate the production of protein tumour markers. Here, we discuss how this new knowledge opens up new perspectives for cancer therapeutics.
[Mh] Termos MeSH primário: Biomarcadores/sangue
Neoplasias/sangue
Proteostase
Resposta a Proteínas não Dobradas
[Mh] Termos MeSH secundário: Seres Humanos
Neoplasias/tratamento farmacológico
Neoplasias/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


  8 / 2641 MEDLINE  
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[PMID]:29272280
[Au] Autor:Yin H; Zhao L; Jiang X; Li S; Huo H; Chen H
[Ad] Endereço:State Key Laboratory of Veterinary Biotechnology, Heilongjiang Provincial Key Laboratory of Laboratory Animal and Comparative Medicine, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Science, Harbin, P. R. China.
[Ti] Título:DEV induce autophagy via the endoplasmic reticulum stress related unfolded protein response.
[So] Source:PLoS One;12(12):e0189704, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Duck enteritis virus (DEV) can infect ducks, geese, and many other poultry species and leads to acute, septic and highly fatal infectious disease. Autophagy is an evolutionarily ancient pathway that plays an important role in many viral infections. We previously reported that DEV infection induces autophagy for its own benefit, but how this occurs remains unclear. In this study, endoplasmic reticulum (ER) stress was triggered by DEV infection, as demonstrated by the increased expression of the ER stress marker glucose-regulated protein 78 (GRP78) and the dilated morphology of the ER. Pathways associated with the unfolded protein response (UPR), including the PKR-like ER protein kinase (PERK) and inositol-requiring enzyme 1 (IRE1) pathways, but not the activating transcription factor 6 (ATF6) pathway, were activated in DEV-infected duck embryo fibroblast (DEF) cells. In addition, the knockdown of both PERK and IRE1 by small interfering RNAs (siRNAs) reduced the level of LC3-II and viral yields, which suggested that the PERK-eukaryotic initiation factor 2α (eIF2α) and IRE1-x-box protein1 (XBP1) pathways may contribute to DEV-induced autophagy. Collectively, these data offer new insight into the mechanisms of DEV -induced autophagy through activation of the ER stress-related UPR pathway.
[Mh] Termos MeSH primário: Autofagia/fisiologia
Estresse do Retículo Endoplasmático
Mardivirus/fisiologia
Resposta a Proteínas não Dobradas
[Mh] Termos MeSH secundário: Animais
Western Blotting
Células Cultivadas
Patos
Eletroforese em Gel de Poliacrilamida
Microscopia Eletrônica de Transmissão
Interferência de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171223
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189704


  9 / 2641 MEDLINE  
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[PMID]:29198525
[Au] Autor:Amin-Wetzel N; Saunders RA; Kamphuis MJ; Rato C; Preissler S; Harding HP; Ron D
[Ad] Endereço:Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, UK.
[Ti] Título:A J-Protein Co-chaperone Recruits BiP to Monomerize IRE1 and Repress the Unfolded Protein Response.
[So] Source:Cell;171(7):1625-1637.e13, 2017 Dec 14.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:When unfolded proteins accumulate in the endoplasmic reticulum (ER), the unfolded protein response (UPR) increases ER-protein-folding capacity to restore protein-folding homeostasis. Unfolded proteins activate UPR signaling across the ER membrane to the nucleus by promoting oligomerization of IRE1, a conserved transmembrane ER stress receptor. However, the coupling of ER stress to IRE1 oligomerization and activation has remained obscure. Here, we report that the ER luminal co-chaperone ERdj4/DNAJB9 is a selective IRE1 repressor that promotes a complex between the luminal Hsp70 BiP and the luminal stress-sensing domain of IRE1α (IRE1 ). In vitro, ERdj4 is required for complex formation between BiP and IRE1 . ERdj4 associates with IRE1 and recruits BiP through the stimulation of ATP hydrolysis, forcibly disrupting IRE1 dimers. Unfolded proteins compete for BiP and restore IRE1 to its default, dimeric, and active state. These observations establish BiP and its J domain co-chaperones as key regulators of the UPR.
[Mh] Termos MeSH primário: Endorribonucleases/metabolismo
Proteínas de Choque Térmico HSP40/metabolismo
Proteínas de Choque Térmico/metabolismo
Proteínas de Membrana/metabolismo
Chaperonas Moleculares/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Resposta a Proteínas não Dobradas
[Mh] Termos MeSH secundário: Animais
Cricetinae
Retículo Endoplasmático/metabolismo
Seres Humanos
Dobramento de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNAJB9 protein, human); 0 (HSP40 Heat-Shock Proteins); 0 (Heat-Shock Proteins); 0 (Membrane Proteins); 0 (Molecular Chaperones); 0 (molecular chaperone GRP78); EC 2.7.11.1 (ERN1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.1.- (Endoribonucleases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE


  10 / 2641 MEDLINE  
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[PMID]:28177127
[Au] Autor:Bohnert KR; McMillan JD; Kumar A
[Ad] Endereço:Department of Anatomical Sciences Neurobiology, University of Louisville School of Medicine, Louisville, Kentucky.
[Ti] Título:Emerging roles of ER stress and unfolded protein response pathways in skeletal muscle health and disease.
[So] Source:J Cell Physiol;233(1):67-78, 2018 Jan.
[Is] ISSN:1097-4652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Skeletal muscle is the most abundant tissue in the human body and can adapt its mass as a consequence of physical activity, metabolism, growth factors, and disease conditions. Skeletal muscle contains an extensive network of endoplasmic reticulum (ER), called sarcoplasmic reticulum, which plays an important role in the regulation of proteostasis and calcium homeostasis. In many cell types, environmental and genetic factors that disrupt ER function cause an accumulation of misfolded and unfolded proteins in the ER lumen that ultimately leads to ER stress. To alleviate the stress and restore homeostasis, the ER activates a signaling network called the unfolded protein response (UPR). The UPR has three arms, which regulate protein synthesis and expression of many ER chaperone and regulatory proteins. However, the role of individual UPR pathways in skeletal muscle has just begun to be investigated. Recent studies suggest that UPR pathways play pivotal roles in muscle stem cell homeostasis, myogenic differentiation, and regeneration of injured skeletal muscle. Moreover, markers of ER stress and the UPR are activated in skeletal muscle in diverse conditions such as exercise, denervation, starvation, high fat diet, cancer cachexia, and aging. Accumulating evidence also suggests that ER stress may have important roles in the pathogenesis of inflammatory myopathies and genetic muscle disorders. The purpose of this review article is to discuss the role and potential mechanisms by which ER stress and the individual arms of the UPR regulate skeletal muscle formation, plasticity, and function in various physiological and pathophysiological conditions.
[Mh] Termos MeSH primário: Estresse do Retículo Endoplasmático
Retículo Endoplasmático/metabolismo
Proteínas Musculares/metabolismo
Músculo Esquelético/metabolismo
Doenças Musculares/metabolismo
Resposta a Proteínas não Dobradas
[Mh] Termos MeSH secundário: Adaptação Fisiológica
Envelhecimento
Animais
Retículo Endoplasmático/patologia
Metabolismo Energético
Exercício
Homeostase
Seres Humanos
Desenvolvimento Muscular
Músculo Esquelético/patologia
Músculo Esquelético/fisiopatologia
Atrofia Muscular/metabolismo
Atrofia Muscular/patologia
Atrofia Muscular/fisiopatologia
Doenças Musculares/patologia
Doenças Musculares/fisiopatologia
Regeneração
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Muscle Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171212
[Lr] Data última revisão:
171212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170209
[St] Status:MEDLINE
[do] DOI:10.1002/jcp.25852



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