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Natural Product Reports May 2015ER stress has been identified as a hallmark, and sometimes trigger, of several pathologies, notably cancer, inflammation and neurodegenerative diseases like Alzheimer's... (Review)
Review
ER stress has been identified as a hallmark, and sometimes trigger, of several pathologies, notably cancer, inflammation and neurodegenerative diseases like Alzheimer's and Parkinson's. Among the molecules described in literature known to affect ER function, the majority are natural products, suggesting that natural molecules may constitute a significant arsenal of chemical entities for modulating this cellular target. In this review, we will start by presenting the current knowledge of ER biology and the hallmarks of ER stress, thus paving the way for presenting the natural products that have been described as being ER modulators, either stress inducers or ER protectors. The chemistry, distribution and mechanism of action of these compounds will be presented and discussed.
Topics: Alzheimer Disease; Animals; Biological Products; Endoplasmic Reticulum; Humans; Molecular Structure; Neurodegenerative Diseases; Parkinson Disease
PubMed: 25703279
DOI: 10.1039/c4np00102h -
Proceedings of the National Academy of... Apr 2022
Topics: Cell Membrane; Endoplasmic Reticulum
PubMed: 35353604
DOI: 10.1073/pnas.2202254119 -
Tanpakushitsu Kakusan Koso. Protein,... Jul 1987
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Proteomics Nov 2010The endoplasmic reticulum (ER) is a multifunctional intracellular organelle responsible for the synthesis, processing and trafficking of a wide variety of proteins... (Review)
Review
The endoplasmic reticulum (ER) is a multifunctional intracellular organelle responsible for the synthesis, processing and trafficking of a wide variety of proteins essential for cell growth and survival. Therefore, comprehensive characterization of the ER proteome is of great importance to the understanding of its functions and has been actively pursued in the past decade by scientists in the proteomics field. This review summarizes major proteomic studies published in the past decade that focused on the ER proteome. We evaluate the data sets obtained from two different organs, liver and pancreas each of which contains a primary cell type (hepatocyte and acinar cell) with specialized functions. We also discuss how the nature of the proteins uncovered is related to the methods of organelle purification, organelle purity and the techniques used for protein separation prior to MS. In addition, this review also puts emphasis on the biological insights gained from these studies regarding the molecular functions of the ER including protein synthesis and translocation, protein folding and quality control, ER-associated degradation and ER stress, ER export and membrane trafficking, calcium homeostasis and detoxification and drug metabolism.
Topics: Animals; Cattle; Cricetinae; Databases, Protein; Dogs; Endoplasmic Reticulum; Humans; Mice; Proteomics; Rats
PubMed: 21080494
DOI: 10.1002/pmic.201000234 -
Biological Research 2011Neurons are highly polarized, but the trafficking mechanisms that operate in these cells and the topological organization of their secretory organelles are still poorly... (Review)
Review
Neurons are highly polarized, but the trafficking mechanisms that operate in these cells and the topological organization of their secretory organelles are still poorly understood. Particularly incipient is our knowledge of the role of the neuronal endoplasmic reticulum. Here we review the current understanding of the endoplasmic reticulum in neurons, its structure, composition, dendritic distribution and dynamics. We also focus on the trafficking of proteins through the dendritic endoplasmic reticulum, emphasizing the relevance of transport, retention, assembly of multi-subunit protein complexes and export. We additionally discuss the roles of the dendritic endoplasmic reticulum in synaptic plasticity.
Topics: Cell Membrane Permeability; Dendrites; Endoplasmic Reticulum; Humans; Membrane Proteins; Neuronal Plasticity; Protein Transport
PubMed: 21720677
DOI: 10.4067/S0716-97602011000100004 -
Molecular Cell Jan 2024Ubiquitin-fold modifier 1 (UFM1) is a ubiquitin-like protein covalently conjugated with intracellular proteins through UFMylation, a process similar to ubiquitylation.... (Review)
Review
Ubiquitin-fold modifier 1 (UFM1) is a ubiquitin-like protein covalently conjugated with intracellular proteins through UFMylation, a process similar to ubiquitylation. Growing lines of evidence regarding not only the structural basis of the components essential for UFMylation but also their biological properties shed light on crucial roles of the UFM1 system in the endoplasmic reticulum (ER), such as ER-phagy and ribosome-associated quality control at the ER, although there are some functions unrelated to the ER. Mouse genetics studies also revealed the indispensable roles of this system in hematopoiesis, liver development, neurogenesis, and chondrogenesis. Of critical importance, mutations of genes encoding core components of the UFM1 system in humans cause hereditary developmental epileptic encephalopathy and Schohat-type osteochondrodysplasia of the epiphysis. Here, we provide a multidisciplinary review of our current understanding of the mechanisms and cellular functions of the UFM1 system as well as its pathophysiological roles, and discuss issues that require resolution.
Topics: Humans; Animals; Mice; Proteins; Ubiquitination; Ubiquitins; Endoplasmic Reticulum; Cell Physiological Phenomena
PubMed: 38141606
DOI: 10.1016/j.molcel.2023.11.034 -
Current Opinion in Structural Biology Feb 2001The endoplasmic reticulum is the entry point into the secretory pathway. To acquire a correct conformation, secretory proteins encounter the endoplasmic reticulum... (Review)
Review
The endoplasmic reticulum is the entry point into the secretory pathway. To acquire a correct conformation, secretory proteins encounter the endoplasmic reticulum molecular machines of folding, quality control, signaling and disposal, which function as an integrated mechanism. The creation of such a molecular network, spatially regulated, suggests how the endoplasmic reticulum promotes the release of correctly folded secretory proteins.
Topics: Endoplasmic Reticulum; Models, Biological; Protein Folding; Protein Transport; Proteins; Signal Transduction
PubMed: 11179901
DOI: 10.1016/s0959-440x(00)00168-8 -
Current Topics in Developmental Biology 2000The endoplasmic reticulum is a multifunctional continuous network of membrane-enclosed sacs and tubules that extends throughout the cell. The endoplasmic reticulum is... (Review)
Review
The endoplasmic reticulum is a multifunctional continuous network of membrane-enclosed sacs and tubules that extends throughout the cell. The endoplasmic reticulum is the site of protein synthesis and assembly, as well as lipid and membrane synthesis. Additionally, the endoplasmic reticulum contains calcium pumps, intraluminal calcium storage proteins, and specific calcium-releasing channels. Thus, this membrane system plays a central role in intracellular signaling through the storage and release of calcium. At fertilization, the sperm triggers a large and dramatic release of calcium from the endoplasmic reticulum, which activates the egg to begin development. The ability of the egg to fully elevate calcium depends on biochemical and structural changes during oocyte maturation. The sensitivity of the calcium-releasing system increases and the endoplasmic reticulum is reorganized during maturation of the oocyte; together, these dynamic changes place a substantial calcium storage compartment just beneath the membrane, near the site of sperm-egg fusion. Localization of the calcium store may also contribute to the long-lasting calcium oscillations that are characteristic of mammalian fertilization. Examination of the endoplasmic reticulum in living eggs is leading to a better understanding of calcium release at fertilization.
Topics: Animals; Calcium; Endoplasmic Reticulum; Humans; Mammals; Oocytes; Ovum
PubMed: 10948453
DOI: 10.1016/s0070-2153(00)50007-6 -
Antioxidants & Redox Signaling Apr 2012
Topics: Animals; Antioxidants; Endoplasmic Reticulum; Humans; Metabolic Networks and Pathways; Oxidants; Oxidation-Reduction
PubMed: 22145591
DOI: 10.1089/ars.2011.4463 -
Die Naturwissenschaften Jul 1975After a general review of enzyme topology and the molecular architecture of endoplasmic reticulum the latest research results are discussed. Microsomal enzymes do not... (Review)
Review
After a general review of enzyme topology and the molecular architecture of endoplasmic reticulum the latest research results are discussed. Microsomal enzymes do not occur in specialized regions of the endoplasmic reticulum but are uniformly distributed over the entire membrane system. Functionally associated enzymes are also located in the direct vicinity of the membrane. It has been shown that the catalytic activity of integral enzyme proteins depends on phospholipid and membrane structure. These membrane-bound lipoproteid complexes exert specific effects as vectorial enzyme catalysts. The endoplasmic reticulum is active is active in the intracellular transport of metabolites.
Topics: Animals; Biological Transport, Active; Endoplasmic Reticulum; Lipoproteins; Liver; Membranes; Microsomes; Rats
PubMed: 1105202
DOI: 10.1007/BF00608893