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Endoplasmic reticulum (ER) is an intracellular organelle responsible for protein folding and assembly, lipid and sterol biosynthesis, and calcium storage. A number of biochemical, physiological, or pathological stimuli can interrupt protein folding process, causing accumulation of unfolded or misfolded proteins in the ER lumen, a condition called “ER stress”. To cope with accumulation of unfolded or misfolded proteins, the ER has evolved a group of signaling pathways termed “Unfolded Protein Response (UPR)” or “ER stress response” to align cellular physiology. To maintain ER homeostasis, transcriptional regulation mediated through multiple UPR branches is orchestrated to increase ER folding capacity, reduce ER workload, and promote degradation of misfolded proteins. In recent years, accumulating evidence suggests that ER stress-triggered transcriptional reprogramming exists in many pathophysiological processes and plays fundamental roles in the initiation and progression of a variety of diseases, such as metabolic disease, cardiovascular disease, neurodegenerative disease, and cancer. Understanding effects and mechanisms of ER stress-associated transcriptional reprogramming has high impact on many areas of molecular genetics and will be particularly informative to the development of pharmacologic avenues towards the prevention and treatment of modern common human diseases by targeting the UPR signaling. For these reasons, ER stress response and transcriptional reprogramming are a timely and necessary topic of discussion for Frontiers in Genetics.
Cytology --- Biology --- Health & Biological Sciences --- ER stress --- Inflammation --- Transcriptional reprogramming --- Unfolded Protein Response --- Metabolism --- Oncogenes
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Environmental stress factors negatively affect plant growth by inducing proteins dysfunction. As coping strategies, plant have developed a comprehensive protein quality controlling system (PQCS) to keep proteins homeostasis. In this research topic of “Protein Quality Controlling Systems in Plant Responses to Environmental Stresses”, some latest researches and opinions in this field, including heat shock proteins (HSPs), unfolded protein response (UPR), ubiquitin-proteasome system (UPS) and autophagy, were reported, aiming to provide novel insights for increasing crop production under environmental challenges.
unfolded protein response --- proteasome --- environmental stress --- autophagy --- plant --- heat shock proteins
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Environmental stress factors negatively affect plant growth by inducing proteins dysfunction. As coping strategies, plant have developed a comprehensive protein quality controlling system (PQCS) to keep proteins homeostasis. In this research topic of “Protein Quality Controlling Systems in Plant Responses to Environmental Stresses”, some latest researches and opinions in this field, including heat shock proteins (HSPs), unfolded protein response (UPR), ubiquitin-proteasome system (UPS) and autophagy, were reported, aiming to provide novel insights for increasing crop production under environmental challenges.
unfolded protein response --- proteasome --- environmental stress --- autophagy --- plant --- heat shock proteins
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Environmental stress factors negatively affect plant growth by inducing proteins dysfunction. As coping strategies, plant have developed a comprehensive protein quality controlling system (PQCS) to keep proteins homeostasis. In this research topic of “Protein Quality Controlling Systems in Plant Responses to Environmental Stresses”, some latest researches and opinions in this field, including heat shock proteins (HSPs), unfolded protein response (UPR), ubiquitin-proteasome system (UPS) and autophagy, were reported, aiming to provide novel insights for increasing crop production under environmental challenges.
unfolded protein response --- proteasome --- environmental stress --- autophagy --- plant --- heat shock proteins
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Unfolded protein response (UPR) is a cellular adaptive response for restoring endoplasmic reticulum (ER) homeostasis in response to ER stress. Perturbation of the UPR and failure to restore ER homeostasis inevitably leads to diseases. It has now become evident that perturbation of the UPR is the cause of many important human diseases such as neurodegenerative diseases, cystic fibrosis, diabetes and cancer. It has recently emerged that virus infections can trigger the UPR but the relationship between virus infections and host UPR is intriguing. On one hand, UPR is harmful to the virus and virus has developed means to subvert the UPR. On the other hand, virus exploits the host UPR to assist in its own infection, gene expression, establishment of persistence, reactivation from latency and to evade the immune response. When this delicate balance of virus-host UPR interaction is broken down, it may cause diseases. This is particularly challenging for viruses that establish a chronic infection to maintain this balance. Each virus interacts with the host UPR in a different way to suit their life style and how the virus interacts with the host UPR can define the characteristic of a particular virus infection. Understanding how a particular virus interacts with the host UPR may pave the way to the design of a new class of anti-viral that targets this particular pathway to skew the response towards anti-virus. This knowledge can also be translated into the clinics to help re-design oncolytic virotherapy and gene therapy. In this research topic we aimed to compile a collection of focused review articles, original research articles, commentary, opinion, hypothesis and methods to highlight the current advances in this burgeoning area of research, in an attempt to provide an in-depth understanding of how viruses interact with the host UPR, which may be beneficial to the future combat of viral and human diseases.
Virus diseases. --- Viruses. --- ERAD --- virus-host interaction --- innate immunity --- Gene Therapy --- Pathogenesis --- Endoplasmic Reticulum Stress --- Unfolded Protein Response --- Autophagy
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Unfolded protein response (UPR) is a cellular adaptive response for restoring endoplasmic reticulum (ER) homeostasis in response to ER stress. Perturbation of the UPR and failure to restore ER homeostasis inevitably leads to diseases. It has now become evident that perturbation of the UPR is the cause of many important human diseases such as neurodegenerative diseases, cystic fibrosis, diabetes and cancer. It has recently emerged that virus infections can trigger the UPR but the relationship between virus infections and host UPR is intriguing. On one hand, UPR is harmful to the virus and virus has developed means to subvert the UPR. On the other hand, virus exploits the host UPR to assist in its own infection, gene expression, establishment of persistence, reactivation from latency and to evade the immune response. When this delicate balance of virus-host UPR interaction is broken down, it may cause diseases. This is particularly challenging for viruses that establish a chronic infection to maintain this balance. Each virus interacts with the host UPR in a different way to suit their life style and how the virus interacts with the host UPR can define the characteristic of a particular virus infection. Understanding how a particular virus interacts with the host UPR may pave the way to the design of a new class of anti-viral that targets this particular pathway to skew the response towards anti-virus. This knowledge can also be translated into the clinics to help re-design oncolytic virotherapy and gene therapy. In this research topic we aimed to compile a collection of focused review articles, original research articles, commentary, opinion, hypothesis and methods to highlight the current advances in this burgeoning area of research, in an attempt to provide an in-depth understanding of how viruses interact with the host UPR, which may be beneficial to the future combat of viral and human diseases.
Virus diseases. --- Viruses. --- ERAD --- virus-host interaction --- innate immunity --- Gene Therapy --- Pathogenesis --- Endoplasmic Reticulum Stress --- Unfolded Protein Response --- Autophagy
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Unfolded protein response (UPR) is a cellular adaptive response for restoring endoplasmic reticulum (ER) homeostasis in response to ER stress. Perturbation of the UPR and failure to restore ER homeostasis inevitably leads to diseases. It has now become evident that perturbation of the UPR is the cause of many important human diseases such as neurodegenerative diseases, cystic fibrosis, diabetes and cancer. It has recently emerged that virus infections can trigger the UPR but the relationship between virus infections and host UPR is intriguing. On one hand, UPR is harmful to the virus and virus has developed means to subvert the UPR. On the other hand, virus exploits the host UPR to assist in its own infection, gene expression, establishment of persistence, reactivation from latency and to evade the immune response. When this delicate balance of virus-host UPR interaction is broken down, it may cause diseases. This is particularly challenging for viruses that establish a chronic infection to maintain this balance. Each virus interacts with the host UPR in a different way to suit their life style and how the virus interacts with the host UPR can define the characteristic of a particular virus infection. Understanding how a particular virus interacts with the host UPR may pave the way to the design of a new class of anti-viral that targets this particular pathway to skew the response towards anti-virus. This knowledge can also be translated into the clinics to help re-design oncolytic virotherapy and gene therapy. In this research topic we aimed to compile a collection of focused review articles, original research articles, commentary, opinion, hypothesis and methods to highlight the current advances in this burgeoning area of research, in an attempt to provide an in-depth understanding of how viruses interact with the host UPR, which may be beneficial to the future combat of viral and human diseases.
Virus diseases. --- Viruses. --- ERAD --- virus-host interaction --- innate immunity --- Gene Therapy --- Pathogenesis --- Endoplasmic Reticulum Stress --- Unfolded Protein Response --- Autophagy
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The secretions of the exocrine pancreas provide for digestion of a meal into components that are then available for processing and absorption by the intestinal epithelium. Without the exocrine pancreas, malabsorption and malnutrition result. This chapter describes the cellular participants responsible for the secretion of digestive enzymes and fluid that in combination provide a pancreatic secretion that accomplishes the digestive functions of the gland. Key cellular participants, the acinar cell and the duct cell, are responsible for digestive enzyme and fluid secretion, respectively, of the exocrine pancreas. This chapter describes the neurohumoral pathways that mediate the pancreatic response to a meal as well as details of the cellular mechanisms that are necessary for the organ responses, including protein synthesis and transport and ion transports, and the regulation of these responses by intracellular signaling systems. Examples of pancreatic diseases resulting from dysfunction in cellular mechanisms provide emphasis of the importance of the normal physiologic mechanisms.
Pancreas. --- Pancreatic acinar cells. --- Pancreas, Exocrine. --- Pancreas --- Secretion --- Digestive enzymes --- Acinar cell --- Duct cell --- Digestion --- Centroacinar cell --- Cholecystokinin --- Secretin --- Endoplasmic reticulum --- Zymogens --- Zymogen granule --- Condensing vacuole --- Lysosome --- Unfolded protein response --- Cystic fibrosis --- Trypsinogen --- Lipase --- Amylase
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The endoplasmic reticulum (ER) is a manufacturing unit in eukaryotic cells required for the synthesis of proteins, lipids, metabolites and hormones. Besides supporting cellular signalling networks by its anabolic function, the ER on its own or in communication with other organelles directly initiates signalling processes of physiological significance. Based on the intimate and immediate involvement in stress signalling the ER is considered as sensory organelle on which cells strongly rely to effectively translate environmental cues into adaptive stress responses. The transcellular distribution of the ER providing comprehensive cell-to-cell connections in multicellular organisms probably allows a concerted action of cell alliances and tissue areas towards environmental constraints. At the cellular level, stress adaptation correlates with the capability of the ER machinery to synthesise proteins participating in stress signalling as well as in the activation of ER membrane localised proteins to start cell-protective signalling processes. Importantly, depending on the stress insult, the ER either supports protective strategies or initiates cell death programmes. Recent, genetic, molecular and cell biological studies have drawn an initial picture of underlying signalling events activated by ER membrane localised proteins. In this Research Topic, we will provide a platform for articles describing research on ER morphology and metabolism with a focus on stress translation. The Research Topic will be sub-divided into the following sections: 1. ER in stress signalling and adaptation; 2. ER structure and biosynthetic functions; 3. Regulation of protein processing; 4. Regulation of programmed cell death.
Endoplasmic reticulum. --- Botany. --- Endoplasmic Reticulum Stress. --- Stress, Endoplasmic Reticulum --- Endoplasmic Reticulum Stresses --- Reticulum Stress, Endoplasmic --- Reticulum Stresses, Endoplasmic --- Stresses, Endoplasmic Reticulum --- Unfolded Protein Response --- Endoplasmic Reticulum-Associated Degradation --- Botanical science --- Floristic botany --- Phytobiology --- Phytography --- Phytology --- Plant biology --- Plant science --- Biology --- Natural history --- Plants --- Cell organelles --- Myosins --- cysteine endopeptidase --- ER associated degradation --- ER bodies --- programmed cell death --- bZIP transcription factors --- caspase
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This book gathers a collection of review articles aiming to provide an update of the current knowledge on PD pathogenesis. It notably includes an overview of several key cellular dysfunctions underlying the etiology of Parkinson’s disease, including ER stress, mitophagy and alpha-synuclein-linked pathology.
Medicine --- Neurosciences --- Parkinson’s disease --- unfolded protein response --- reticulum endoplasmic --- genetics --- alpha-synuclein --- prion-like spreading --- cell-to-cell transfer --- neurodegeneration --- mitochondrial dysfunction --- PINK1 --- neurons --- astrocytes --- microglia --- α-synuclein --- exocytosis --- lipids --- membranes --- Parkinson disease --- SNARE complex --- synapse --- vesicle fusion --- therapeutic target --- protein quality control --- mitochondrial quality control --- ubiquitin --- alpha-syn --- mitophagy --- Parkin --- mito-Keima --- mito-QC --- mito-SRAI
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