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Journal articles on the topic 'ATF6α'

Author: Grafiati

Published: 7 December 2024

Last updated: 31 July 2025

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1

Davis, Emery, Mohammad-Reza Shokri, Mary B. Rowland та ін. "ATF6β is not essential for the development of physiological cardiac hypertrophy". PLOS ONE 20, № 4 (2025): e0320178. https://doi.org/10.1371/journal.pone.0320178.

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Physiological cardiac hypertrophy is a compensatory remodeling of the heart in response to stimuli such as exercise training or pregnancy that is reversible and well-tolerated. We previously described how the activating transcription factor 6 (ATF6) proteins, ATF6α and ATF6β, were required for pathological hypertrophy in response to hemodynamic stress. Here, we examine the functional roles of both ATF6 proteins in the context of exercise-induced physiological hypertrophy. After 20 days of swim training, we found differential roles: whole body gene-deleted mice lacking ATF6α had an attenuated h

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2

Amyot, Julie, Isma Benterki, Ghislaine Fontés, et al. "Binding of activating transcription factor 6 to the A5/Core of the rat insulin II gene promoter does not mediate its transcriptional repression." Journal of Molecular Endocrinology 47, no. 3 (2011): 273–83. http://dx.doi.org/10.1530/jme-11-0016.

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Pancreatic β-cells have a well-developed endoplasmic reticulum due to their highly specialized secretory function to produce insulin in response to glucose and nutrients. It has been previously reported that overexpression of activating transcription factor 6 (ATF6) reduces insulin gene expression in part via upregulation of small heterodimer partner. In this study, we investigated whether ATF6 directly binds to the insulin gene promoter, and whether its direct binding represses insulin gene promoter activity. A bioinformatics analysis identified a putative ATF6 binding site in the A5/Core reg

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Yoshida, Hiderou, Tetsuya Okada, Kyosuke Haze та ін. "Endoplasmic Reticulum Stress-Induced Formation of Transcription Factor Complex ERSF Including NF-Y (CBF) and Activating Transcription Factors 6α and 6β That Activates the Mammalian Unfolded Protein Response". Molecular and Cellular Biology 21, № 4 (2001): 1239–48. http://dx.doi.org/10.1128/mcb.21.4.1239-1248.2001.

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ABSTRACT The levels of molecular chaperones and folding enzymes in the endoplasmic reticulum (ER) are controlled by a transcriptional induction process termed the unfolded protein response (UPR). The mammalian UPR is mediated by the cis-acting ER stress response element (ERSE), the consensus sequence of which is CCAAT-N9-CCACG. We recently proposed that ER stress response factor (ERSF) binding to ERSE is a heterologous protein complex consisting of the constitutive component NF-Y (CBF) binding to CCAAT and an inducible component binding to CCACG and identified the basic leucine zipper-type tra

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Lee, Ann-Hwee, Neal N. Iwakoshi, and Laurie H. Glimcher. "XBP-1 Regulates a Subset of Endoplasmic Reticulum Resident Chaperone Genes in the Unfolded Protein Response." Molecular and Cellular Biology 23, no. 21 (2003): 7448–59. http://dx.doi.org/10.1128/mcb.23.21.7448-7459.2003.

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ABSTRACT The mammalian unfolded protein response (UPR) protects the cell against the stress of misfolded proteins in the endoplasmic reticulum (ER). We have investigated here the contribution of the UPR transcription factors XBP-1, ATF6α, and ATF6β to UPR target gene expression. Gene profiling of cell lines lacking these factors yielded several XBP-1-dependent UPR target genes, all of which appear to act in the ER. These included the DnaJ/Hsp40-like genes, p58IPK, ERdj4, and HEDJ, as well as EDEM, protein disulfide isomerase-P5, and ribosome-associated membrane protein 4 (RAMP4), whereas expre

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Ishikawa, Tokiro, Tetsuya Okada, Tomoko Ishikawa-Fujiwara та ін. "ATF6α/β-mediated adjustment of ER chaperone levels is essential for development of the notochord in medaka fish". Molecular Biology of the Cell 24, № 9 (2013): 1387–95. http://dx.doi.org/10.1091/mbc.e12-11-0830.

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ATF6α and ATF6β are membrane-bound transcription factors activated by regulated intramembrane proteolysis in response to endoplasmic reticulum (ER) stress to induce various ER quality control proteins. ATF6α- and ATF6β single-knockout mice develop normally, but ATF6α/β double knockout causes embryonic lethality, the reason for which is unknown. Here we show in medaka fish that ATF6α is primarily responsible for transcriptional induction of the major ER chaperone BiP and that ATF6α/β double knockout, but not ATF6α- or ATF6β single knockout, causes embryonic lethality, as in mice. Analyses of ER

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Sharma, Rohit B., Christine Darko, and Laura C. Alonso. "Intersection of the ATF6 and XBP1 ER stress pathways in mouse islet cells." Journal of Biological Chemistry 295, no. 41 (2020): 14164–77. http://dx.doi.org/10.1074/jbc.ra120.014173.

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Success or failure of pancreatic beta cell adaptation to ER stress is a determinant of diabetes susceptibility. The ATF6 and IRE1/XBP1 pathways are separate ER stress-response effectors important to beta cell health and function. ATF6α. and XBP1 direct overlapping transcriptional responses in some cell types. However, the signaling dynamics and interdependence of ATF6α and XBP1 in pancreatic beta cells have not been explored. To assess pathway-specific signal onset, we performed timed exposures of primary mouse islet cells to ER stressors and measured the early transcriptional response. Compar

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Teodoro, Tracy, Tanya Odisho, Elena Sidorova та Allen Volchuk. "Pancreatic β-cells depend on basal expression of active ATF6α-p50 for cell survival even under nonstress conditions". American Journal of Physiology-Cell Physiology 302, № 7 (2012): C992—C1003. http://dx.doi.org/10.1152/ajpcell.00160.2011.

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Activating transcription factor 6 (ATF6) is one of three principle endoplasmic reticulum (ER) stress response proteins and becomes activated when ER homeostasis is perturbed. ATF6 functions to increase ER capacity by stimulating transcription of ER-resident chaperone genes such as GRP78. Using an antibody that recognizes active ATF6α-p50, we found that active ATF6α was detected in insulinoma cells and rodent islets even under basal conditions and the levels were further increased by ER stress. To examine the function of ATF6α-p50, we depleted endogenous ATF6α-p50 levels using small interfering

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8

Xue, Fei, Jianwen Lu, Samuel C. Buchl та ін. "Coordinated signaling of activating transcription factor 6α and inositol-requiring enzyme 1α regulates hepatic stellate cell-mediated fibrogenesis in mice". American Journal of Physiology-Gastrointestinal and Liver Physiology 320, № 5 (2021): G864—G879. http://dx.doi.org/10.1152/ajpgi.00453.2020.

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ATF6α is a critical driver of hepatic stellate cell (HSC) activation in vitro. HSC-specific deletion of Atf6a limits fibrogenesis in vivo despite increased IRE1α signaling. Conditional deletion of Ire1α from HSCs limits fibrogenic gene transcription without impacting overall fibrosis. This could be due in part to observed upregulation of the ATF6α pathway. Dual loss of Atf6a and Ire1a from HSCs worsens fibrosis in vivo through enhanced HSC activation.

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Stauffer, Winston T., Adrian Arrieta, Erik A. Blackwood та Christopher C. Glembotski. "Sledgehammer to Scalpel: Broad Challenges to the Heart and Other Tissues Yield Specific Cellular Responses via Transcriptional Regulation of the ER-Stress Master Regulator ATF6α". International Journal of Molecular Sciences 21, № 3 (2020): 1134. http://dx.doi.org/10.3390/ijms21031134.

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There are more than 2000 transcription factors in eukaryotes, many of which are subject to complex mechanisms fine-tuning their activity and their transcriptional programs to meet the vast array of conditions under which cells must adapt to thrive and survive. For example, conditions that impair protein folding in the endoplasmic reticulum (ER), sometimes called ER stress, elicit the relocation of the ER-transmembrane protein, activating transcription factor 6α (ATF6α), to the Golgi, where it is proteolytically cleaved. This generates a fragment of ATF6α that translocates to the nucleus, where

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Azuma, Yoshinori, Daisuke Hagiwara, Wenjun Lu та ін. "Activating Transcription Factor 6α Is Required for the Vasopressin Neuron System to Maintain Water Balance Under Dehydration in Male Mice". Endocrinology 155, № 12 (2014): 4905–14. http://dx.doi.org/10.1210/en.2014-1522.

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Activating transcription factor 6α (ATF6α) is a sensor of endoplasmic reticulum (ER) stress and increases the expression of ER chaperones and molecules related to the ER-associated degradation of unfolded/misfolded proteins. In this study, we used ATF6α knockout (ATF6α−/−) mice to clarify the role of ATF6α in the arginine vasopressin (AVP) neuron system. Although urine volumes were not different between ATF6α−/− and wild-type (ATF6α+/+) mice with access to water ad libitum, they were increased in ATF6α−/− mice compared with those in ATF6α+/+ mice under intermittent water deprivation (WD) and a

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Pagliara, Valentina, Giuseppina Amodio, Vincenzo Vestuto та ін. "Myogenesis in C2C12 Cells Requires Phosphorylation of ATF6α by p38 MAPK". Biomedicines 11, № 5 (2023): 1457. http://dx.doi.org/10.3390/biomedicines11051457.

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Activating transcription factor 6α (ATF6α) is an endoplasmic reticulum protein known to participate in unfolded protein response (UPR) during ER stress in mammals. Herein, we show that in mouse C2C12 myoblasts induced to differentiate, ATF6α is the only pathway of the UPR activated. ATF6α stimulation is p38 MAPK-dependent, as revealed by the use of the inhibitor SB203580, which halts myotube formation and, at the same time, impairs trafficking of ATF6α, which accumulates at the cis-Golgi without being processed in the p50 transcriptional active form. To further evaluate the role of ATF6α, we k

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12

HAZE, Kyosuke, Tetsuya OKADA, Hiderou YOSHIDA, et al. "Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of the mammalian unfolded protein response." Biochemical Journal 355, no. 1 (2001): 19–28. http://dx.doi.org/10.1042/bj3550019.

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Eukaryotic cells control the levels of molecular chaperones and folding enzymes in the endoplasmic reticulum (ER) by a transcriptional induction process termed the unfolded protein response (UPR). The mammalian UPR is mediated by the cis-acting ER stress response element consisting of 19nt (CCAATN9CCACG), the CCACG part of which is considered to provide specificity. We recently identified the basic leucine zipper (bZIP) protein ATF6 as a mammalian UPR-specific transcription factor; ATF6 is activated by ER stress-induced proteolysis and binds directly to CCACG. Here we report that eukaryotic ce

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Ekong, Udeme D., Jie Yao, James Knight, et al. "HERV1-env dependent unfolded protein response activation is a potential initiator of autoreactivity in autoimmune liver disease." Journal of Immunology 204, no. 1_Supplement (2020): 224.7. http://dx.doi.org/10.4049/jimmunol.204.supp.224.7.

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Abstract Regulatory T cells are not terminally differentiated but can acquire effector properties. Here we report Human Endogenous Retrovirus 1 (HERV1-env) induction of endoplasmic reticulum (ER) stress with Unfolded Protein Response (UPR) activation, through its interaction with ATF6. UPR activation cleaves ATF6 to its α and β isoforms. ATF6α up-regulates RORC, STAT3 and TBX21 and induces IL-17A and INF-γ production in regulatory T cells by binding to promoter sequences. Silencing of HERV1-env results in partial recovery of regulatory T cell suppressive function and abrogation of apoptosis. T

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Thuerauf, Donna J., Lisa Morrison та Christopher C. Glembotski. "Opposing Roles for ATF6α and ATF6β in Endoplasmic Reticulum Stress Response Gene Induction". Journal of Biological Chemistry 279, № 20 (2004): 21078–84. http://dx.doi.org/10.1074/jbc.m400713200.

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He, Yanfeng, Shigeo Sato, Chieri Tomomori-Sato та ін. "Elongin functions as a loading factor for Mediator at ATF6α-regulated ER stress response genes". Proceedings of the National Academy of Sciences 118, № 39 (2021): e2108751118. http://dx.doi.org/10.1073/pnas.2108751118.

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The bZIP transcription factor ATF6α is a master regulator of endoplasmic reticulum (ER) stress response genes. In this report, we identify the multifunctional RNA polymerase II transcription factor Elongin as a cofactor for ATF6α-dependent transcription activation. Biochemical studies reveal that Elongin functions at least in part by facilitating ATF6α-dependent loading of Mediator at the promoters and enhancers of ER stress response genes. Depletion of Elongin from cells leads to impaired transcription of ER stress response genes and to defects in the recruitment of Mediator and its CDK8 kina

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Yamamoto, Keisuke, Kazuna Takahara, Seiichi Oyadomari та ін. "Induction of Liver Steatosis and Lipid Droplet Formation in ATF6α-Knockout Mice Burdened with Pharmacological Endoplasmic Reticulum Stress". Molecular Biology of the Cell 21, № 17 (2010): 2975–86. http://dx.doi.org/10.1091/mbc.e09-02-0133.

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Accumulation of unfolded proteins in the endoplasmic reticulum (ER) activates homeostatic responses collectively termed the unfolded protein response. Among the three principal signaling pathways operating in mammals, activating transcription factor (ATF)6α plays a pivotal role in transcriptional induction of ER-localized molecular chaperones and folding enzymes as well as components of ER-associated degradation, and thereby mouse embryonic fibroblasts deficient in ATF6α are sensitive to ER stress. However, ATF6α-knockout mice show no apparent phenotype under normal growing conditions. In this

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Kim, Ju Won, So-Hyun Bae, Yesol Moon та ін. "Transcriptomic analysis of cellular senescence induced by ectopic expression of ATF6α in human breast cancer cells". PLOS ONE 19, № 10 (2024): e0309749. http://dx.doi.org/10.1371/journal.pone.0309749.

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Background The transcriptomic profile of cellular senescence is strongly associated with distinct cell types, the specific stressors triggering senescence, and temporal progression through senescence stages. This implies the potential necessity of conducting separate investigations for each cell type and a stressor inducing senescence. To elucidate the molecular mechanism that drives endoplasmic reticulum (ER) stress-induced cellular senescence in MCF-7 breast cancer cells, with a particular emphasis on the ATF6α branch of the unfolded protein response. We conducted transcriptomic analysis on

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Ninagawa, Satoshi, Tetsuya Okada, Yoshiki Sumitomo, et al. "Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathway." Journal of Cell Biology 211, no. 4 (2015): 775–84. http://dx.doi.org/10.1083/jcb.201504109.

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Glycoproteins and non-glycoproteins possessing unfolded/misfolded parts in their luminal regions are cleared from the endoplasmic reticulum (ER) by ER-associated degradation (ERAD)-L with distinct mechanisms. Two-step mannose trimming from Man9GlcNAc2 is crucial in the ERAD-L of glycoproteins. We recently showed that this process is initiated by EDEM2 and completed by EDEM3/EDEM1. Here, we constructed chicken and human cells simultaneously deficient in EDEM1/2/3 and analyzed the fates of four ERAD-L substrates containing three potential N-glycosylation sites. We found that native but unstable

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Sundaram, Arunkumar, Suhila Appathurai, Rachel Plumb та Malaiyalam Mariappan. "Dynamic changes in complexes of IRE1α, PERK, and ATF6α during endoplasmic reticulum stress". Molecular Biology of the Cell 29, № 11 (2018): 1376–88. http://dx.doi.org/10.1091/mbc.e17-10-0594.

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The endoplasmic reticulum (ER) localized unfolded protein response (UPR) sensors, IRE1α, PERK, and ATF6α, are activated by the accumulation of misfolded proteins in the ER. It is unclear how the endogenous UPR sensors are regulated by both ER stress and the ER luminal chaperone BiP, which is a negative regulator of UPR sensors. Here we simultaneously examined the changes in the endogenous complexes of UPR sensors by blue native PAGE immunoblotting in unstressed and stressed cells. We found that all three UPR sensors exist as preformed complexes even in unstressed cells. While PERK complexes sh

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Forouhan, M., K. Mori та R. P. Boot-Handford. "Paradoxical roles of ATF6α and ATF6β in modulating disease severity caused by mutations in collagen X". Matrix Biology 70 (вересень 2018): 50–71. http://dx.doi.org/10.1016/j.matbio.2018.03.004.

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Guan, Dongyin, Hao Wang, Veronica E. Li, Yingying Xu, Min Yang та Zonghou Shen. "N-glycosylation of ATF6β is essential for its proteolytic cleavage and transcriptional repressor function to ATF6α". Journal of Cellular Biochemistry 108, № 4 (2009): 825–31. http://dx.doi.org/10.1002/jcb.22310.

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Bobrovnikova-Marjon, Ekaterina, та J. Alan Diehl. "Coping with Stress: ATF6α Takes the Stage". Developmental Cell 13, № 3 (2007): 322–24. http://dx.doi.org/10.1016/j.devcel.2007.08.006.

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Liu, Pingting, Md Razaul Karim, Ana Covelo, Yuan Yue, Michael K. Lee, and Wensheng Lin. "The UPR Maintains Proteostasis and the Viability and Function of Hippocampal Neurons in Adult Mice." International Journal of Molecular Sciences 24, no. 14 (2023): 11542. http://dx.doi.org/10.3390/ijms241411542.

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The unfolded protein response (UPR), which comprises three branches: PERK, ATF6α, and IRE1, is a major mechanism for maintaining cellular proteostasis. Many studies show that the UPR is a major player in regulating neuron viability and function in various neurodegenerative diseases; however, its role in neurodegeneration is highly controversial. Moreover, while evidence suggests activation of the UPR in neurons under normal conditions, deficiency of individual branches of the UPR has no major effect on brain neurons in animals. It remains unclear whether or how the UPR participates in regulati

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MARUYAMA, Ryuto, Yuki KAMOSHIDA, Makoto SHIMIZU, Jun INOUE та Ryuichiro SATO. "ATF6α Stimulates Cholesterogenic Gene Expression andde NovoCholesterol Synthesis". Bioscience, Biotechnology, and Biochemistry 77, № 8 (2013): 1734–38. http://dx.doi.org/10.1271/bbb.130295.

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Arai, Masaaki, Nobuo Kondoh, Nobuo Imazeki та ін. "Transformation-associated gene regulation by ATF6α during hepatocarcinogenesis". FEBS Letters 580, № 1 (2005): 184–90. http://dx.doi.org/10.1016/j.febslet.2005.11.072.

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Walter, Franziska, Aisling O'Brien, Caoimhín G. Concannon, Heiko Düssmann та Jochen H. M. Prehn. "ER stress signaling has an activating transcription factor 6α (ATF6)-dependent “off-switch”". Journal of Biological Chemistry 293, № 47 (2018): 18270–84. http://dx.doi.org/10.1074/jbc.ra118.002121.

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In response to an accumulation of unfolded proteins in the endoplasmic reticulum (ER) lumen, three ER transmembrane signaling proteins, inositol-requiring enzyme 1 (IRE1), PRKR-like ER kinase (PERK), and activating transcription factor 6α (ATF6α), are activated. These proteins initiate a signaling and transcriptional network termed the unfolded protein response (UPR), which re-establishes cellular proteostasis. When this restoration fails, however, cells undergo apoptosis. To investigate cross-talk between these different UPR enzymes, here we developed a high-content live cell screening platfo

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Papp, Sylvia, Xiaochu Zhang, Eva Szabo, Marek Michalak, and Michal Opas. "Expression of Endoplasmic Reticulum Chaperones in Cardiac Development." Open Cardiovascular Medicine Journal 2, no. 1 (2008): 31–35. http://dx.doi.org/10.2174/1874192400802010031.

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To determine if cardiogenesis causes endoplasmic reticulum stress, we examined chaperone expression. Many cardiac pathologies cause activation of the fetal gene program, and we asked the reverse: could activation of the fetal gene program during development induce endoplasmic reticulum stress/chaperones? We found stress related chaperones were more abundant in embryonic compared to adult hearts, indicating endoplasmic reticulum stress during normal cardiac development. To determine the degree of stress, we investigated endoplasmic reticulum stress pathways during cardiogenesis. We detected hig

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Jao, Tzu-Ming, Masaomi Nangaku, Chia-Hsien Wu та ін. "ATF6α downregulation of PPARα promotes lipotoxicity-induced tubulointerstitial fibrosis". Kidney International 95, № 3 (2019): 577–89. http://dx.doi.org/10.1016/j.kint.2018.09.023.

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Jin, Byungseok, Tokiro Ishikawa, Makoto Kashima та ін. "Activation of XBP1 but not ATF6α rescues heart failure induced by persistent ER stress in medaka fish". Life Science Alliance 6, № 7 (2023): e202201771. http://dx.doi.org/10.26508/lsa.202201771.

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The unfolded protein response is triggered in vertebrates by ubiquitously expressed IRE1α/β (although IRE1β is gut-specific in mice), PERK, and ATF6α/β, transmembrane-type sensor proteins in the ER, to cope with ER stress, the accumulation of unfolded and misfolded proteins in the ER. Here, we burdened medaka fish, a vertebrate model organism, with ER stress persistently from fertilization by knocking out theAXERgene encoding an ATP/ADP exchanger in the ER membrane, leading to decreased ATP concentration–mediated impairment of the activity of Hsp70- and Hsp90-type molecular chaperones in the E

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Gjymishka, Altin, Nan Su, and Michael S. Kilberg. "Transcriptional induction of the human asparagine synthetase gene during the unfolded protein response does not require the ATF6 and IRE1/XBP1 arms of the pathway." Biochemical Journal 417, no. 3 (2009): 695–703. http://dx.doi.org/10.1042/bj20081706.

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The UPR (unfolded protein response) pathway comprises three signalling cascades mediated by the ER (endoplasmic reticulum) stress-sensor proteins PERK [PKR (double-stranded RNA-activated protein kinase)-like ER kinase], IRE1 (inositol-requiring kinase 1) and ATF6 (activating transcription factor 6). The present study shows that ASNS (asparagine synthetase) transcription activity was up-regulated in HepG2 cells treated with the UPR activators thapsigargin and tunicamycin. ChIP (chromatin immunoprecipitation) analysis demonstrated that during ER stress, ATF4, ATF3 and C/EBPβ (CCAAT/enhancer-bind

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Thuerauf, Donna J., Marie Marcinko, Peter J. Belmont та Christopher C. Glembotski. "Effects of the Isoform-specific Characteristics of ATF6α and ATF6β on Endoplasmic Reticulum Stress Response Gene Expression and Cell Viability". Journal of Biological Chemistry 282, № 31 (2007): 22865–78. http://dx.doi.org/10.1074/jbc.m701213200.

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Druelle, Clémentine, Claire Drullion, Julie Deslé та ін. "ATF6α regulates morphological changes associated with senescence in human fibroblasts". Oncotarget 7, № 42 (2016): 67699–715. http://dx.doi.org/10.18632/oncotarget.11505.

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Kezuka, Dai, Mika Tkarada-Iemata, Tsuyoshi Hattori та ін. "Deletion of Atf6α enhances kainate-induced neuronal death in mice". Neurochemistry International 92 (січень 2016): 67–74. http://dx.doi.org/10.1016/j.neuint.2015.12.009.

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Sharma, Rohit B., Jarin T. Snyder та Laura C. Alonso. "Atf6α impacts cell number by influencing survival, death and proliferation". Molecular Metabolism 27 (вересень 2019): S69—S80. http://dx.doi.org/10.1016/j.molmet.2019.06.005.

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Xue, Fei, Harmeet Malhi, Vijay Shah та Jessica L. Maiers. "Su1691 ATF6α SIGNALING IS CRUCIAL FOR HSC ACTIVATION AND FIBROGENESIS". Gastroenterology 158, № 6 (2020): S—1383—S—1384. http://dx.doi.org/10.1016/s0016-5085(20)34126-3.

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Kim, Hee Suk, Yongjin Kim, Min Jae Lim, Yun-Gyu Park, Serk In Park та Jeongwon Sohn. "The p38‐activated ER stress‐ATF6α axis mediates cellular senescence". FASEB Journal 33, № 2 (2018): 2422–34. http://dx.doi.org/10.1096/fj.201800836r.

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Potes, Yaiza, Beatriz De Luxán-Delgado, Adrian Rubio-González, Russel J. Reiter, and Ana Maria Coto Montes. "Dose-dependent beneficial effect of melatonin on obesity; interaction of melatonin and leptin." Melatonin Research 2, no. 1 (2019): 1–8. http://dx.doi.org/10.32794/mr11250008.

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Although numerous studies have noted leptin’s role in obesity, there are still important mechanisms insights that need to be elucidated. Disturbed leptin production is associated with eating disorders, leading to alter food intake and energy expenditure. Proper regulation of protein homeostasis is critical for metabolic diseases such as obesity. Thus, the purpose of the present work was to study the unfolded protein response, which is implicated in the alleviation of endoplasmic reticulum stress-dependent dysregulation of nutritional status. We studied the effect of leptin deficiency on liver,

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Baumeister, Peter, Shengzhan Luo, William C. Skarnes, et al. "Endoplasmic Reticulum Stress Induction of the Grp78/BiP Promoter: Activating Mechanisms Mediated by YY1 and Its Interactive Chromatin Modifiers." Molecular and Cellular Biology 25, no. 11 (2005): 4529–40. http://dx.doi.org/10.1128/mcb.25.11.4529-4540.2005.

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ABSTRACT The unfolded protein response is an evolutionarily conserved mechanism whereby cells respond to stress conditions that target the endoplasmic reticulum (ER). The transcriptional activation of the promoter of GRP78/BiP, a prosurvival ER chaperone, has been used extensively as an indicator of the onset of the UPR. YY1, a constitutively expressed multifunctional transcription factor, activates the Grp78 promoter only under ER stress conditions. Previously, in vivo footprinting analysis revealed that the YY1 binding site of the ER stress response element of the Grp78 promoter exhibits ER

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Akai, Ryoko, Hisayo Hamashima, Michiko Saito, Kenji Kohno та Takao Iwawaki. "Partial limitation of cellular functions and compensatory modulation of unfolded protein response pathways caused by double-knockout of ATF6α and ATF6β". Cell Stress and Chaperones 29, № 1 (2024): 34–48. http://dx.doi.org/10.1016/j.cstres.2023.11.002.

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Meco, Giuseppe. "The role of ATF6α in protecting dopaminergic neurons form MPTP toxicity". Movement Disorders 26, № 3 (2011): 378. http://dx.doi.org/10.1002/mds.23636.

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Peng, Chiung-Chi, Chang-Rong Chen, Chang-Yu Chen, Yen-Chung Lin, Kuan-Chou Chen та Robert Y. Peng. "Nifedipine Upregulates ATF6-α, Caspases -12, -3, and -7 Implicating Lipotoxicity-Associated Renal ER Stress". International Journal of Molecular Sciences 21, № 9 (2020): 3147. http://dx.doi.org/10.3390/ijms21093147.

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Abstract:

Nifedipine (NF) is reported to have many beneficial effects in antihypertensive therapy. Recently, we found that NF induced lipid accumulation in renal tubular cells. Palmitic acid-induced renal lipotoxicity was found to be partially mediated by endoplasmic reticular (ER) stress, while it can also be elicited by NF in kidney cells; we examined the induction of suspected pathways in both in vitro and in vivo models. NRK52E cells cultured in high-glucose medium were treated with NF (30 µM) for 24–48 h. ER stress-induced lipotoxicity was explored by staining with thioflavin T and Nile red, transm

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Egawa, Naohiro, Keisuke Yamamoto, Haruhisa Inoue та ін. "The Endoplasmic Reticulum Stress Sensor, ATF6α, Protects against Neurotoxin-induced Dopaminergic Neuronal Death". Journal of Biological Chemistry 286, № 10 (2010): 7947–57. http://dx.doi.org/10.1074/jbc.m110.156430.

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Lu, Wenjun, Daisuke Hagiwara, Yoshiaki Morishita та ін. "Unfolded protein response in hypothalamic cultures of wild-type and ATF6α-knockout mice". Neuroscience Letters 612 (січень 2016): 199–203. http://dx.doi.org/10.1016/j.neulet.2015.12.031.

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Egawa, Naohiro, Keisuke Yamamoto, Haruhisa Inoue, Katsunori Nishi, Kazutoshi Mori та Ryosuke Takahashi. "The role of ER stress sensor ATF6α in the pathogenesis of Parkinson's disease". Neuroscience Research 65 (січень 2009): S118. http://dx.doi.org/10.1016/j.neures.2009.09.554.

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Soczewski, E., S. Gori, D. Paparini та ін. "VIP conditions human endometrial receptivity by privileging endoplasmic reticulum stress through ATF6α pathway". Molecular and Cellular Endocrinology 516 (жовтень 2020): 110948. http://dx.doi.org/10.1016/j.mce.2020.110948.

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Unno, Hirotoshi, Marina Miller, Peter Rosenthal, Andrew Beppu, Sudipta Das та David H. Broide. "Activating transcription factor 6α (ATF6α) regulates airway hyperreactivity, smooth muscle proliferation, and contractility". Journal of Allergy and Clinical Immunology 141, № 1 (2018): 439–42. http://dx.doi.org/10.1016/j.jaci.2017.07.053.

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Wu, Jun, D. Thomas Rutkowski, Meghan Dubois та ін. "ATF6α Optimizes Long-Term Endoplasmic Reticulum Function to Protect Cells from Chronic Stress". Developmental Cell 13, № 3 (2007): 351–64. http://dx.doi.org/10.1016/j.devcel.2007.07.005.

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Lowe, C. E., R. J. Dennis, U. Obi, S. O'Rahilly та J. J. Rochford. "Investigating the involvement of the ATF6α pathway of the unfolded protein response in adipogenesis". International Journal of Obesity 36, № 9 (2011): 1248–51. http://dx.doi.org/10.1038/ijo.2011.233.

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Fernandez-Fernandez, Maria Rosario, Isidro Ferrer та Jose J. Lucas. "Impaired ATF6α processing, decreased Rheb and neuronal cell cycle re-entry in Huntington's disease". Neurobiology of Disease 41, № 1 (2011): 23–32. http://dx.doi.org/10.1016/j.nbd.2010.08.014.

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Yarapureddy, Suma, Jazmine Abril, Janet Foote та ін. "ATF6α Activation Enhances Survival against Chemotherapy and Serves as a Prognostic Indicator in Osteosarcoma". Neoplasia 21, № 6 (2019): 516–32. http://dx.doi.org/10.1016/j.neo.2019.02.004.

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