Relevant bibliographies by topics / Endoplasmic Reticulum

Academic literature on the topic 'Endoplasmic Reticulum'

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Published: 4 June 2021
Last updated: 6 July 2024

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Journal articles on the topic "Endoplasmic Reticulum"

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Koch, G., M. Smith, D. Macer, P. Webster, and R. Mortara. "Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin." Journal of Cell Science 86, no. 1 (December 1, 1986): 217–32. http://dx.doi.org/10.1242/jcs.86.1.217.

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The most abundant protein in microsomal membrane preparations from mammalian cells has been identified as a 100 X 10(3) Mr concanavalin A-binding glycoprotein. The glycosyl moiety of the glycoprotein is completely sensitive to endoglycosidase H, suggesting a predominantly endoplasmic reticulum localization in the cell. Using a monospecific antibody it was shown by binding and immunofluorescence studies that the glycoprotein is intracellular. Immunoelectron microscopy showed that the glycoprotein was at least 100 times more concentrated in the endoplasmic reticulum than in any other cellular organelle. It was found to be substantially overexpressed in cells and tissues rich in endoplasmic reticulum. Since it is the major common protein component associated with the endoplasmic reticulum we refer to it as endoplasmin. Calcium-binding studies show that endoplasmin is a major calcium-binding protein in cells, suggesting that at least one of its roles might be in the calcium-storage function of the endoplasmic reticulum. The amino-terminal sequence of endoplasmin is identical to that of a 100 X 10(3) Mr stress-related protein.
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Deneke, Jurgen. "Endoplasmic reticulum." Biochemical Society Transactions 28, no. 3 (June 1, 2000): A59. http://dx.doi.org/10.1042/bst028a059.

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Arozarena, Imanol, David Matallanas, María T. Berciano, Victoria Sanz-Moreno, Fernando Calvo, María T. Muñoz, Gustavo Egea, Miguel Lafarga, and Piero Crespo. "Activation of H-Ras in the Endoplasmic Reticulum by the RasGRF Family Guanine Nucleotide Exchange Factors." Molecular and Cellular Biology 24, no. 4 (February 15, 2004): 1516–30. http://dx.doi.org/10.1128/mcb.24.4.1516-1530.2004.

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ABSTRACT Recent findings indicate that in addition to its location in the peripheral plasma membrane, H-Ras is found in endomembranes like the endoplasmic reticulum and the Golgi complex. In these locations H-Ras is functional and can efficiently engage downstream effectors, but little is known about how its activation is regulated in these environments. Here we show that the RasGRF family exchange factors, both endogenous and ectopically expressed, are present in the endoplasmic reticulum but not in the Golgi complex. With the aid of H-Ras constructs specifically tethered to the plasma membrane, endoplasmic reticulum, and Golgi complex, we demonstrate that RasGRF1 and RasGRF2 can activate plasma membrane and reticular, but not Golgi-associated, H-Ras. We also show that RasGRF DH domain is required for the activation of H-Ras in the endoplasmic reticulum but not in the plasma membrane. Furthermore, we demonstrate that RasGRF mediation favors the activation of reticular H-Ras by lysophosphatidic acid treatment whereas plasma membrane H-Ras is made more responsive to stimulation by ionomycin. Overall, our results provide the initial insights into the regulation of H-Ras activation in the endoplasmic reticulum.
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BANHEGYI, G., P. BAUMEISTER, A. BENEDETTI, D. DONG, Y. FU, A. S. LEE, J. LI, et al. "Endoplasmic Reticulum Stress." Annals of the New York Academy of Sciences 1113, no. 1 (May 18, 2007): 58–71. http://dx.doi.org/10.1196/annals.1391.007.

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Terasaki, M., and T. S. Reese. "Characterization of endoplasmic reticulum by co-localization of BiP and dicarbocyanine dyes." Journal of Cell Science 101, no. 2 (February 1, 1992): 315–22. http://dx.doi.org/10.1242/jcs.101.2.315.

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The original concept of endoplasmic reticulum derived from the observation of a reticular network in cultured fibroblasts by electron microscopy of whole cells. It was previously reported that the fluorescent dye, DiOC6(3), stains a similar network as well as mitochondria and other organelles in living cells. Here, we investigate the significance of the structures labeled by DiO6(3) in CV-1 cells, a monkey epithelial cell line. First, we show that the network stained in living CV-1 cells is preserved by glutaraldehyde fixation and then we co-label it with an antibody against BiP (immunoglobulin binding protein), a protein commonly accepted to be present in the endoplasmic reticulum. Anti-BiP labeled the same network as that labeled by DiOC6(3), so this network now is identified as being part of the endoplasmic reticulum. DiOC6(3) labels many other membrane compartments in addition to the endoplasmic reticulum. This, along with its lipophilic properties, suggests that DiOC6(3) stains all intracellular membranes. However, the extensive reticular network in the thin peripheral regions of cultured cells is easily distinguished from these other membranes. Thus, staining by DiOC6(3) is a useful method for localizing the endoplasmic reticulum, particularly in thin peripheral regions of cultured cells.
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Villa, Antonello, Paola Podini, Alessandra Nori, Maria Carla Panzeri, Adelina Martini, Jacopo Meldolesi, and Pompeo Volpe. "The Endoplasmic Reticulum-Sarcoplasmic Reticulum Connection." Experimental Cell Research 209, no. 1 (November 1993): 140–48. http://dx.doi.org/10.1006/excr.1993.1294.

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Zhou, Long-Xia, An-Ning Yang, Jiu-Kai Chen, Li Zhao, Yan-Hua Wang, Xian-Mei Liu, Xin Cai, Ming-Hao Zhang, Yi-Deng Jiang, and Jun Cao. "Endoplasmic reticulum oxidoreductin 1α mediates homocysteine-induced hepatocyte endoplasmic reticulum stress." World Chinese Journal of Digestology 22, no. 34 (2014): 5228. http://dx.doi.org/10.11569/wcjd.v22.i34.5228.

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Kumar, Ravindra, Bandana Kumari, and Manish Kumar. "Prediction of endoplasmic reticulum resident proteins using fragmented amino acid composition and support vector machine." PeerJ 5 (September 4, 2017): e3561. http://dx.doi.org/10.7717/peerj.3561.

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BackgroundThe endoplasmic reticulum plays an important role in many cellular processes, which includes protein synthesis, folding and post-translational processing of newly synthesized proteins. It is also the site for quality control of misfolded proteins and entry point of extracellular proteins to the secretory pathway. Hence at any given point of time, endoplasmic reticulum contains two different cohorts of proteins, (i) proteins involved in endoplasmic reticulum-specific function, which reside in the lumen of the endoplasmic reticulum, called as endoplasmic reticulum resident proteins and (ii) proteins which are in process of moving to the extracellular space. Thus, endoplasmic reticulum resident proteins must somehow be distinguished from newly synthesized secretory proteins, which pass through the endoplasmic reticulum on their way out of the cell. Approximately only 50% of the proteins used in this study as training data had endoplasmic reticulum retention signal, which shows that these signals are not essentially present in all endoplasmic reticulum resident proteins. This also strongly indicates the role of additional factors in retention of endoplasmic reticulum-specific proteins inside the endoplasmic reticulum.MethodsThis is a support vector machine based method, where we had used different forms of protein features as inputs for support vector machine to develop the prediction models. During trainingleave-one-outapproach of cross-validation was used. Maximum performance was obtained with a combination of amino acid compositions of different part of proteins.ResultsIn this study, we have reported a novel support vector machine based method for predicting endoplasmic reticulum resident proteins, named as ERPred. During training we achieved a maximum accuracy of 81.42% withleave-one-outapproach of cross-validation. When evaluated on independent dataset, ERPred did prediction with sensitivity of 72.31% and specificity of 83.69%. We have also annotated six different proteomes to predict the candidate endoplasmic reticulum resident proteins in them. A webserver, ERPred, was developed to make the method available to the scientific community, which can be accessed athttp://proteininformatics.org/mkumar/erpred/index.html.DiscussionWe found that out of 124 proteins of the training dataset, only 66 proteins had endoplasmic reticulum retention signals, which shows that these signals are not an absolute necessity for endoplasmic reticulum resident proteins to remain inside the endoplasmic reticulum. This observation also strongly indicates the role of additional factors in retention of proteins inside the endoplasmic reticulum. Our proposed predictor, ERPred, is a signal independent tool. It is tuned for the prediction of endoplasmic reticulum resident proteins, even if the query protein does not contain specific ER-retention signal.
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Groenendyk, Jody, Xiao Fan, Zhenling Peng, Lukasz Kurgan, and Marek Michalak. "Endoplasmic reticulum and the microRNA environment in the cardiovascular system." Canadian Journal of Physiology and Pharmacology 97, no. 6 (June 2019): 515–27. http://dx.doi.org/10.1139/cjpp-2018-0720.

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Stress responses are important to human physiology and pathology, and the inability to adapt to cellular stress leads to cell death. To mitigate cellular stress and re-establish homeostasis, cells, including those in the cardiovascular system, activate stress coping response mechanisms. The endoplasmic reticulum, a component of the cellular reticular network in cardiac cells, mobilizes so-called endoplasmic reticulum stress coping responses, such as the unfolded protein response. MicroRNAs play an important part in the maintenance of cellular and tissue homeostasis, perform a central role in the biology of the cardiac myocyte, and are involved in pathological cardiac function and remodeling. In this paper, we review a link between endoplasmic reticulum homeostasis and microRNA with an emphasis on the impact on stress responses in the cardiovascular system.
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Römisch, Karin. "ENDOPLASMIC RETICULUM–ASSOCIATED DEGRADATION." Annual Review of Cell and Developmental Biology 21, no. 1 (November 2005): 435–56. http://dx.doi.org/10.1146/annurev.cellbio.21.012704.133250.

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Dissertations / Theses on the topic "Endoplasmic Reticulum"

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Calì, Tito. "Tuning endoplasmic reticulum associated degradation /." [S.l.] : [s.n.], 2008. http://www.zb.unibe.ch/download/eldiss/08cali_t.pdf.

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Wahlman, Judit. "Fluorescent-detected retrotranslocation of an endoplasmic reticulum - associated degradation (ERAD) substrate in a mammalian in vitro system." Diss., Texas A&M University, 2007. http://hdl.handle.net/1969.1/85786.

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Secretory proteins that are unable to assemble into native proteins in the endoplasmic reticulum (ER) are transported back into the cytosol for degradation. Many cytosolic and ER resident proteins have been identified so far as being involved in this retrotranslocation process, but it is difficult to determine whether these proteins have a direct or indirect effect. Interpretations are further complicated if the loss of a specific protein is obscured by the presence of another protein that is partially or wholly redundant. To overcome these limitations, a mammalian in vitro system was developed that allowed to monitor retrotranslocation synchronously and in real time in the absence of concurrent translocation. To examine the roles of different components in ER-associated degradation (ERAD), well-defined and homogeneous mammalian ER microsomes were prepared biochemically by encapsulating a fluorescent-labeled ERAD substrate with specific lumenal components. After mixing ATP, specific cytosolic proteins, and specific fluorescence quenching agents with microsomes, substrate retrotranslocation was initiated. The rate of substrate efflux from microsomes was monitored spectroscopically and continuously in real time by the reduction in fluorescence intensity as the fluorescent substrates passed through the ER membrane and were exposed to the quenching agents. Retrotranslocation kinetics were not significantly altered by replacing all lumenal proteins with only protein disulfide isomerase, or all cytosolic proteins with only the 19S proteasome cap. Retrotranslocation was blocked by affinity-purified antibodies against Derlin1, but not by affinity-purified antibodies against Sec61α or by membrane-bound ribosomes. Since the substrate also photocrosslinked Derlin1, but not Sec61α or TRAM, retrotranslocation of this ERAD substrate apparently involves Derlin1, but not the translocon. By labeling either the C- or N-terminus, it was revealed that the N-terminus of one ERAD substrate leaves the ER lumen first. This finding suggests that the protein is retrotranslocated as a linear polymer in a preferred direction. When RRMs were reconstituted with a fluorescent-labeled ERAD substrate and various ions. Ca2+ ions in the ER lumen increased the rate and extent of retrotranslocation, while Ca2+ ions in the cytosol decreased retrotranslocation. This approach therefore provides the first direct evidence of the involvement and importance of specific ionic requirements for ERAD.
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Bouchekhima, Abdnacer. "Quantification of the plant endoplasmic reticulum." Thesis, University of Warwick, 2009. http://wrap.warwick.ac.uk/2742/.

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One of the challenges of quantitative approaches to biological sciences is the lack of understanding of the interplay between form and function. Each cell is full of complex-shaped objects, which moreover change their form over time. To address this issue, we exploit recent advances in confocal microscopy, by using data collected from a series of optical sections taken at short regular intervals along the optical axis to reconstruct the Endoplasmic Reticulum (ER) in 3D, obtain its skeleton, then associate to each of its edges key geometric and dynamic characteristics obtained from the original filled in ER specimen. These properties include the total length, surface area, and volume of the ER specimen, as well as the length surface area, and volume of each of its branches. In a view to benefit from the well established graph theory algorithms, we abstract the obtained skeleton by a mathematical entity that is a graph. We achieve this by replacing the inner points in each edge in the skeleton by the line segment connecting its end points. We then attach to this graph the ER geometric properties as weights, allowing therefore a more precise quantitative characterisation, by thinning the filled in ER to its essential features. The graph plays a major role in this study and is the final and most abstract quantification of the ER. One of its advantages is that it serves as a geometric invariant, both in static and dynamic samples. Moreover, graph theoretic features, such as the number of vertices and their degrees, and the number of edges and their lengths are robust against different kinds of small perturbations. We propose a methodology to associate parameters such as surface areas and volumes to its individual edges and monitor their variations with time. One of the main contributions of this thesis is the use of the skeleton of the ER to analyse the trajectories of moving junctions using confocal digital videos. We report that the ER could be modeled by a network of connected cylinders (0.87μm±0.36 in diameter) with a majority of 3-way junctions. The average length, surface area and volume of an ER branch are found to be 2.78±2.04μm, 7.53±5.59μm2 and 1.81±1.86μm3 respectively. Using the analysis of variance technique we found that there are no significant differences in four different locations across the cell at 0.05 significance level. The apparent movement of the junctions in the plant ER consists of different types, namely: (a) the extension and shrinkage of tubules, and (b) the closing and opening of loops. The average velocity of a junction is found to be 0.25μm/sec±0.23 and lies in the range 0 to 1.7μm/sec which matches the reported actin filament range.
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Dykstra, Kaitlyn M. "Yip1A structures the mammalian endoplasmic reticulum." Research Showcase @ CMU, 2012. http://repository.cmu.edu/dissertations/140.

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The mammalian endoplasmic reticulum (ER) is the largest organelle in the cell, extending from the nuclear envelope throughout the cell periphery. The ER houses a wide variety of vital cell processes within a single membrane bound organelle. In order to accommodate these functions and respond to the demands of the cell, the ER is partitioned into dynamically regulated subdomains, each with its own distinct structure. Despite the likely importance of ER structure for its functions, few proteins have been identified as having a direct role in maintaining the structure of the ER and the consequences of alteration of normal ER structure are not well understood. Here we identify Yip1A, a conserved membrane protein that cycles between the ER and early Golgi, as a likely regulator of ER organization. Yip1A depletion led to restructuring of ER membranes into micrometer-sized, concentrically stacked whorls. These structures are reminiscent of the ER whorls found in certain specialized secretory cell types, where the regulation and functional consequence of ER whorl formation is not understood. We found that membrane stacking and whorl formation after Yip1A depletion coincided with a marked slowing of coat protein (COP) II-mediated protein export from the ER. Furthermore, whorl formation driven by exogenous expression of an ER protein with no role in COPII function also delayed cargo export. Thus, it appears that Yip1A is required to prevent ER whorl formation and that whorl formation can in turn delay protein export from the organelle. Whether this is the function of ER whorls in tissues remains to be seen, however these results make Yip1A a good candidate for playing a role in their regulation. To obtain insight into how Yip1A regulates ER whorl formation and to determine whether the mechanism might be shared with the yeast homologue Yip1p, we carried out a systematic mutational analysis of all residues in the protein. Two discrete sites (E95 and K146) were crucial for the control of ER whorl formation by Yip1A. Notably, the same residues were previously shown to be important for Yip1p-mediated viability in yeast, indicating a shared mechanism. On the other hand, a third site (E89) also essential for yeast viability was dispensable for Yip1A function in regulating whorl formation. Thus Yip1p/Yip1A may possess at least two distinct essential functions only one of which is required for regulation of ER structure. Of note, the sites required for control of ER whorl formation by Yip1A were dispensable for the binding of Yip1p to its established binding partners Yif1p and Ypt1/31p, whereas the site required for Yip1p to bind the same partners was dispensable for ER structuring by Yip1A. Based on these observations, we speculate that the function of Yip1A in regulating whorl formation is mediated by one or more distinct and yet-to-be identified binding partners. Collectively, these findings indicate that a dispersed ER network is important for proper COPII-mediated protein export and that Yip1A has a conserved function between yeast and humans in maintaining proper ER network dispersal through prevention of ER whorl formation. These studies set up an important framework for determining the molecular mechanism of Yip1A as an ER structuring protein
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Morin-Leisk, Jeanne. "NDKB and Atlastin Structure Endoplasmic Reticulum Membranes." Research Showcase @ CMU, 2011. http://repository.cmu.edu/dissertations/153.

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Of the membrane bound organelles in eukaryotic cells, the endoplasmic reticulum (ER) may be the most complex. It is the largest both in terms of surface area and volume. It includes several subdomains: the nuclear envelope (NE) as well as an extensive network of both highly inter-connected fenestrated tubular membranes and flat cisternal sheets (1, 2). While the structure and organization of the ER is thought to be important for the execution of a myriad of essential cellular functions including protein and lipid synthesis and export as well as calcium sequestration and drug metabolism (3), how this membrane system is generated and maintained despite continuous turnover is only just beginning to be unraveled (4). The microtubule cytoskeleton and molecular motors are clearly important for the extension of tubules from the existing network so that they may fuse with nearby ER tubules to generate new three-way junctions (5-8). However, an ER-like network can be generated in vitro in the absence of microtubules (9), which suggests the existence of additional mechanisms for the extension and scaffolding of the ER network. Once the tubular ER does extend out from the existing network the next critical step is fusion. Soluble NSF attachment-protein receptors (SNAREs) were an obvious candidate for this role (10), but ER homotypic fusion events have not yet been found to depend on SNAREs. Recently, a member of the dynamin super-family of large GTPases, atlastin, was implicated in ER homotypic fusion. An in vitro fusion assay (11) and knockdown experiments (12) in conjunction with the crystal structures of the soluble domains of atlastin (13, 14) have led to a possible mechanism of ER fusion, but this model remains to be tested. In my thesis I will describe two projects. One focuses on the role and mechanism of nucleoside diphosphate kinase B (NDKB) in ER network extension and stabilization. The other focuses on the role and mechanism of atlastin in fusing ER membranes. NDKB was initially implicated as a stimulator of ER export in permeabilized cells (15). Subsequent work suggested that its effect on ER export might be through an effect on ER network morphology. Through in vitro assays, we found that NDKB not only stabilizes the ER network but also actively promotes ER network extension. In order to perform this function we hypothesized that it might interact directly with ER membranes. Indeed, we found a pair of positively charged residues that mediated direct binding of NDKB to anionic phospholipids. When these residues ware mutated to negatively charged residues, NDKB no longer bound anionic phospholipids and failed to mediate ER extension in our semi-intact cell assay. In order to gain insight into the mechanism for how NDKB might be performing its ER network extension function we took another in vitro approach. Anionic synthetic liposomes were incubated with NDKB and we found that NDKB was able to arrange these liposomes into large arrays that resembled the ER network. Together these results implicate NDKB and anionic phospholipids in a role for ER network morphology, in particular as a means to stabilize and extend the ER network. We initially became interested in the atlastin GTPase as a result of an ER overexpression phenotype observed by the Blackstone lab indicating a potential role in ER morphogenesis (16). In strong support for a required role for atlastin in ER structuring, we found that siRNA depletion of atlastin from HeLa cells resulted in a reduction in network density which could be rescued by the addition of an siRNA immune atlastin transgene. This established a structure function assay we could use to dissect the functional domains of atlastin. Concurrent with our identification of key residues required for atlastin function, it was observed by another lab that atlastin could fuse synthetic liposomes (11), suggesting that the ER structuring role we had observed for atlastin might correspond to the membrane fusion step. Simultaneously, structure determinations for the soluble domain of atlastin were reported (13, 14). Together, the collective data suggested the following model for atlastin: GTP dependent dimerization of atlastin leads to tethering and subsequent GTP hydrolysis leads to a large conformational change that drives membrane fusion (13, 14). To test the model, we exploited our identification of a required salt bridge central to the large conformational change proposed to convert GTP-bound tethered atlastin dimers into a postfusion state. We established that although blocking the salt bridge had no effect on GTP binding and hydrolysis, it abolished stable atlastin dimer formation. Then, through a series of crosslinking assays probing the conformational state of the atlastin soluble domain, we showed that atlastin adopts the postfusion conformation in the GTP bound state, without the need for GTP hydrolysis. As a result of our studies, we have modified the current model for atlastin’s function. In our revised model, GTP binding is required for atlastin’s initial dimerization and begins a cascade of conformational changes that results in the large rearrangement thought to drive membrane fusion. We speculate based on our work that hydrolysis may be necessary to complete the fusion cycle and/or function to disassemble the postfusion complex for multiple rounds of fusion. In summary, these studies provide both an initial analysis of a protein with an ER network extension role and important insights into the mechanism of ER membrane fusion. It is hoped that this work will add to our understanding of the biogenesis and maintenance of the ER network.
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Guna, Alina-Ioana. "Membrane protein biosynthesis at the endoplasmic reticulum." Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/276678.

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The biosynthesis of integral membrane proteins (IMPs) is an essential cellular process. IMPs comprise roughly 20-30% of the protein coding genes of all organisms, nearly all of which are inserted and assembled at the endoplasmic reticulum (ER). The defining structural feature of IMPs is one or more transmembrane domains (TMDs). TMDs are typically stretches of predominately hydrophobic amino acids that span the lipid bilayer of biological membranes as an alpha helix. TMDs are remarkably diverse in terms of their topological and biophysical properties. In order to accommodate this diversity, the cell has evolved different sets of machinery that cater to particular subsets of proteins. Our knowledge of how the TMDs of IMPs are selectively recognized, chaperoned into the lipid bilayer, and assembled remains incomplete. This thesis is broadly interested in investigating how TMDs are correctly inserted and assembled at the ER. To address this the biosynthesis of multi-pass IMPs was first considered. Multi-pass IMPs contain two to more than twenty TMDs, with TMDs that vary dramatically in terms of their biophysical properties such as hydrophobicity, length, and helical propensity. The beta-1 adrenergic receptor (β1-AR), a member of the G-protein-coupled receptor (GPCR) family was established as a model substrate in an in vitro system where the insertion and folding of its TMDs could be interrogated. Assembly of β1-AR is not a straightforward process, and current models of insertion fail to explain how the known translocation machinery correctly identifies, inserts, and assembles β1-AR TMDs. An in vivo screen in mammalian cells was therefore conducted to identify additional factors which may be important for multi-pass IMP assembly. The ER membrane protein complex (EMC), a well conserved ER-resident complex of unknown biochemical function, was identified as a promising hit potentially involved in this assembly process. The complexity of working with multi-pass IMPs in an in vitro system prompted the investigation of a simpler class of proteins. Tail-anchored proteins (TA) are characterized by a single C-terminal hydrophobic domain that anchors them into membranes. Though structurally simpler compared to multi-pass IMPs, the TMDs of TA proteins are similarly diverse. We found that known TA insertion pathways fail to engage low-to-moderately hydrophobic TMDs. Instead, these are chaperoned in the cytosol by calmodulin (CaM). Transient release from CaM allows substrates to sample the ER, where resident machinery mediates the insertion reaction. The EMC was shown to be necessary for the insertion of these substrates both in vivo and in vitro. Purified EMC in synthetic liposomes catalysed insertion of its TA substrates in a fully reconstituted system to near-native levels. Therefore, the EMC was rigorously established as a TMD insertase. This key functional insight may explain its critical role in the assembly of multi- pass IMPs – which is now amenable to biochemical dissection.
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Sarkar, Deboleena Dipak. "Potential Role Of Endoplasmic Reticulum Redox Changes In Endoplasmic Reticulum Stress And Impaired Protein Folding In Obesity-Associated Insulin Resistance." Diss., The University of Arizona, 2013. http://hdl.handle.net/10150/306999.

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Endoplasmic reticulum (ER) stress plays an important role in the pathogenesis of obesity-related inflammation and insulin resistance in adipose tissue. However, the mechanisms responsible for induction of ER stress are presently unclear. Proper ER redox state is crucial for oxidative protein folding and secretion and impaired protein folding in ER leads to induction of unfolded protein response and ER stress. However, while ER redox state is more oxidizing compared to the rest of the cell, its regulation is poorly understood. In order to determine the effects of ER redox state on development of ER stress and insulin resistance, several fluorescence-based sensors have been developed. However, these sensors have yielded results that are inconsistent with each other and with earlier non-fluorescence-based studies. In this study we attempted to develop and characterize a sensitive tool to study the ER redox state in adipocytes in real-time by targeting a new generation of redox-sensitive green fluorescent protein (roGFP) to ER. The roGFP1-iL sensor targeted to the ER is termed ‘eroGFP1-iL’ by convention. The ER-targeting eroGFP1-iL construct contains the signal peptide from adiponectin and the ER retention motif KDEL and has a midpoint reduction potential of -229 mV in vitro in oxidized and reduced lipoic acid. Despite having a midpoint reduction potential that is 50 mV higher than the previously determined midpoint reduction potential of the ER, eroGFP1-iL was found capable of detecting both oxidizing and reducing changes in the ER. In an attempt to determine the mechanisms by which roGFP1-iL detects oxidizing changes, we found that, first, glutathione mediated the formation of disulfide-bonded roGFP1-iL dimers with an intermediate excitation fluorescence spectrum resembling a mixture of oxidized and reduced monomers. Second, glutathione facilitated dimerization of roGFP1-iL, which in effect shifted the equilibrium from oxidized monomers to dimers, thereby increasing the molecule’s reduction potential compared with a dithiol redox buffer like lipoic acid. From this study, we concluded that the glutathione redox couple in ER significantly raised the reduction potential of roGFP1-iL in vivo by facilitating its dimerization while preserving its ratiometric nature, which makes it suitable for monitoring oxidizing and reducing changes in ER with high reliability in real-time. The ability of roGFP1-iL to detect both oxidizing and reducing changes in ER and its dynamic response in glutathione redox buffer between approximately -190 and -130 mV in vitro suggest a range of ER redox potential consistent with those determined by earlier approaches that did not involve fluorescent sensors. Our primary aim in developing eroGFP1-iL as a redox-sensing tool was to be able to assess whether redox changes represent an early initiator of ER stress in obesity-induced reduction in high molecular weight (HMW) adiponectin in circulation. Hypoxia is a known mediator of redox changes. We found that oligomerization of HMW adiponectin was impaired in the hypoxic conditions observed in differentiated fat cells. The redox-active antioxidant ascorbate was found capable of reversing hypoxia-induced ER stress. Lastly, we demonstrated that changes in ER redox condition is associated with ER stress response and is implicated in the mechanism of action of the insulin-sensitizing agent troglitazone and desensitizing agent palmitate. Using the redox sensing property of eroGFP1-iL, palmitate was found to be an effective modulator of redox changes in the ER and troglitazone was found to cause oxidizing changes in the ER. The action of palmitate in causing aberrant ER redox conditions was associated with aberrant HMW adiponectin multimerization. Palmitate-induced ER stress was ameliorated by troglitazone. Taken together, the data suggest a potential role of ER redox changes in ER stress and impaired protein folding in adipocytes.
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Hessa, Tara. "Integration of Transmembrane Helices into the Endoplasmic Reticulum /." Stockholm : Department of Biochemistry and Biophysics, Stockholm university, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1229.

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Cunnea, Paula. "Characterisation of the novel endoplasmic reticulum chaperone ERDJ5 /." Stockholm, 2006. http://diss.kib.ki.se/2006/91-7357-044-3/.

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Chen, Leanna. "Construction of a comprehensive yeast endoplasmic reticulum interactome." Thesis, McGill University, 2009. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=66950.

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Abstract:
Protein-protein interactions in the endoplasmic reticulum (ER) are essential for concerted action of higher molecular complexes. However, the presence of transmembrane domains (TMDs) in many ER proteins and the environmental conditions of the ER prohibit protein-protein interactions from being identified in the ER. To detect interactions between membrane and luminal proteins of the ER, the ER Membrane Yeast Two-Hybrid (MYTH) system uses the ER type 1 membrane protein Ire1p as a reporter of protein interactions in the ER. A hyperactive Ire1p system was developed to determine the C-terminal topologies of ER and ER-related proteins to generate functional N-terminal fusions to Ire1p for the MYTH system. Among 256 proteins, which were hard to analyze on a high-throughput basis by other approaches, 454 interactions were identified. Results showed novel links between previously established biological processes, such as that between the SRP-dependent and independent pathways, and provided roles for ER and ER-related proteins.
Les interactions protéine-protéine dans le réticulum endoplasmique (RE) sont essentielles pour qu'une action concertée des complexes moléculaires de haut poids ait lieu. Cependant, la présence de domaines transmembranaires dans plusieurs protéines et les conditions environnementales du RE ne permettent pas l'identification des interactions protéine-protéine dans cette organite. Afin de détecter les interactions entre les protéines membranaires et luminales du RE, nous avons utilisé la technique du MYTHS (Membrane Yeast Two-Hybrid System) qui emploie la protéine membranaire de type 1, Ire1p, comme rapporteur des interactions des protéines dans le RE. Un système du Ire1p hyperactif a été développé afin de déterminer la topologie de l'extrémité C-terminale des protéines du RE ainsi que celles qui sont y reliées en les fusionnant à l'extrémité N-terminale du Ire1p du MYTHS. Parmi les 256 protéines qui étaient difficiles à analyser par d'autres méthodes à haut débit, 454 interactions sont identifiées. Les résultats démontrent des nouveaux liens entre les fonctions biologiques déjà établies comme celles entre les voies dépendantes et indépendantes de la particule de reconnaissance du signal (SRP) et postulent des rôles aux protéines du RE ainsi qu'à celles qui y sont reliées.
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Books on the topic "Endoplasmic Reticulum"

1

Borgese, N., and J. R. Harris, eds. Endoplasmic Reticulum. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2912-5.

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N, Borgese, and Harris J. R, eds. Endoplasmic reticulum. New York: Plenum Press, 1993.

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Hawes, Chris, and Verena Kriechbaumer, eds. The Plant Endoplasmic Reticulum. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7389-7.

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Robinson, David G., ed. The Plant Endoplasmic Reticulum. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/11309680.

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Kriechbaumer, Verena, ed. The Plant Endoplasmic Reticulum. New York, NY: Springer US, 2024. http://dx.doi.org/10.1007/978-1-0716-3710-4.

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A, Benedetti, Bánhegyi Gábor, Burchell A, and NATO Public Diplomacy Division, eds. Endoplasmic reticulum: A metabolic compartment. Amsterdam: IOS Press, 2005.

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Agellon, Luis B., and Marek Michalak, eds. Cellular Biology of the Endoplasmic Reticulum. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-67696-4.

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Richard, Zimmermann. Protein transport into the endoplasmic reticulum. Austin, Tex: Landes Bioscience, 2009.

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D, Zimmermann Richard Ph, ed. Protein transport into the endoplasmic reticulum. Austin, Tex: Landes Bioscience, 2009.

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D, Zimmermann Richard Ph, ed. Protein transport into the endoplasmic reticulum. Austin, Tex: Landes Bioscience, 2009.

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Book chapters on the topic "Endoplasmic Reticulum"

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Jones, R. L. "Endoplasmic Reticulum." In Cell Components, 304–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-82587-3_15.

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Dashek, William V. "Endoplasmic reticulum." In Plant Cells and their Organelles, 42–60. Chichester, UK: John Wiley & Sons, Ltd, 2016. http://dx.doi.org/10.1002/9781118924846.ch3.

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Gooch, Jan W. "Endoplasmic Reticulum." In Encyclopedic Dictionary of Polymers, 889–90. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13649.

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Pavelka, Margit, and Jürgen Roth. "Smooth Endoplasmic Reticulum." In Functional Ultrastructure, 42–43. Vienna: Springer Vienna, 2010. http://dx.doi.org/10.1007/978-3-211-99390-3_23.

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van Vliet, Alex, and Patrizia Agostinis. "Endoplasmic Reticulum Stress." In Encyclopedia of Cancer, 1–7. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_1888-2.

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Chao, Jesse T., and Christopher J. R. Loewen. "Endoplasmic Reticulum Junctions." In Cellular Domains, 177–93. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118015759.ch11.

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Groenendyk, Jody, and Marek Michalak. "The Endoplasmic Reticulum." In Cellular Domains, 113–31. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118015759.ch7.

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Dunford, James C., Louis A. Somma, David Serrano, C. Roxanne Rutledge, John L. Capinera, Guy Smagghe, Eli Shaaya, et al. "Endoplasmic Reticulum (ER)." In Encyclopedia of Entomology, 1322. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6359-6_3574.

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van Vliet, Alex, and Patrizia Agostinis. "Endoplasmic Reticulum Stress." In Encyclopedia of Cancer, 1519–25. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-46875-3_1888.

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Agostinis, Patrizia. "Endoplasmic Reticulum Stress." In Encyclopedia of Cancer, 1240–44. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_1888.

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Conference papers on the topic "Endoplasmic Reticulum"

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Ponomareva, A. A., S. A. Dmitrieva, and F. V. Minibaeva. "Endoplasmic reticulum: stress from stress." In IX Congress of society physiologists of plants of Russia "Plant physiology is the basis for creating plants of the future". Kazan University Press, 2019. http://dx.doi.org/10.26907/978-5-00130-204-9-2019-361.

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Song, Yue, Yueqi Wang, and Yikai Jiang. "Endoplasmic reticulum stress and related diseases." In Third International Conference on Biological Engineering and Medical Science (ICBioMed2023), edited by Alan Wang. SPIE, 2024. http://dx.doi.org/10.1117/12.3021655.

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O’reilly, S. "P105 Endoplasmic reticulum stress mediates dermal fibrosis." In 38th European Workshop for Rheumatology Research, 22–24 February 2018, Geneva, Switzerland. BMJ Publishing Group Ltd and European League Against Rheumatism, 2018. http://dx.doi.org/10.1136/annrheumdis-2018-ewrr2018.121.

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O’reilly, S. "AB0196 Endoplasmic reticulum stress in systemic sclerosis." In Annual European Congress of Rheumatology, EULAR 2018, Amsterdam, 13–16 June 2018. BMJ Publishing Group Ltd and European League Against Rheumatism, 2018. http://dx.doi.org/10.1136/annrheumdis-2018-eular.6443.

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Hassan, Ihab, Michael S. Zhang, Linda S. Powers, Kevin L. Legge, and Martha M. Monick. "Influenza A Infection Modulates Endoplasmic Reticulum Stress." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a1805.

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Ma, X., E. Dobrinskikh, J. S. Kurche, I. T. Stancil, E. Kim, I. V. Yang, and D. A. Schwartz. "Endoplasmic Reticulum Stress in MUC5B-Driven Lung Fibrosis." In American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a4216.

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De Angelis, A., A. Denzi, C. Merla, F. M. Andre, T. Garcia-Sanchez, L. M. Mir, F. Apollonio, and M. Liberti. "Microdosimetric Realistic Model of a Cell with Endoplasmic Reticulum." In 2019 41st Annual International Conference of the IEEE Engineering in Medicine & Biology Society (EMBC). IEEE, 2019. http://dx.doi.org/10.1109/embc.2019.8857540.

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Massaeli, Hamid, Divya Viswanathan, Dhanya Pillai, and Nasrin Mesaeli. "Regulation Of Caveolin-dependent Endocytosis By Endoplasmic Reticulum Chaperones." In Qatar Foundation Annual Research Conference Proceedings. Hamad bin Khalifa University Press (HBKU Press), 2014. http://dx.doi.org/10.5339/qfarc.2014.hbpp1034.

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Delbrel, E., P. S. Fenwick, C. Wrench, J. R. Baker, L. E. Donnelly, and P. J. Barnes. "Endoplasmic reticulum stress implication in fibroblast senescence in COPD." In ERS Lung Science Conference 2020 abstracts. European Respiratory Society, 2020. http://dx.doi.org/10.1183/23120541.lsc-2020.97.

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Chen, Haoyi. "Review on the Endoplasmic Reticulum Stress and Related Diseases." In IMIP '21: 2021 3rd International Conference on Intelligent Medicine and Image Processing. New York, NY, USA: ACM, 2021. http://dx.doi.org/10.1145/3468945.3468972.

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Reports on the topic "Endoplasmic Reticulum"

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Boston, Rebecca S. Coordination of Endoplasmic Reticulum (ER) Signaling During Maize Seed Development. Office of Scientific and Technical Information (OSTI), November 2010. http://dx.doi.org/10.2172/992863.

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Murphy-Ullrich, Joanne E. The Endoplasmic Reticulum Stress Protein Calreticulin in Diabetic Chronic Kidney Disease. Fort Belvoir, VA: Defense Technical Information Center, July 2015. http://dx.doi.org/10.21236/ada624022.

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Burke, Robert E. Endoplasmic Reticulum Stress as a Mediator of Neurotoxin-Induced Dopamine Neuron Death. Fort Belvoir, VA: Defense Technical Information Center, July 2004. http://dx.doi.org/10.21236/ada430729.

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Burke, Robert E. Endoplasmic Reticulum Stress as a Mediator of Neurotoxin-Induced Dopamine Neuron Death. Fort Belvoir, VA: Defense Technical Information Center, July 2006. http://dx.doi.org/10.21236/ada462341.

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Burke, Robert E. Endoplasmic Reticulum Stress as a Mediator of Neurotoxin-Induced Dopamine Neuron Death. Fort Belvoir, VA: Defense Technical Information Center, July 2007. http://dx.doi.org/10.21236/ada476094.

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Kridel, Steven J. Fatty Acid Synthase Inhibitors Engage the Cell Death Program Through the Endoplasmic Reticulum. Fort Belvoir, VA: Defense Technical Information Center, December 2008. http://dx.doi.org/10.21236/ada499919.

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Kridel, Steven J. Fatty Acid Synthase Inhibitors Engage the Cell Death Program Through the Endoplasmic Reticulum. Fort Belvoir, VA: Defense Technical Information Center, December 2007. http://dx.doi.org/10.21236/ada478197.

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Yang, Zeng-Quan, and Kezhong Zhang. Endoplasmic Reticulum-Associated Degradation Factor ERLIN2: Oncogenic Roles and Molecular Targeting of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, June 2012. http://dx.doi.org/10.21236/ada613824.

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Yang, Zeng-Quan, and Kezhong Zhang. Endoplasmic Reticulum-Associated Degradation Factor ERLIN2: Oncogenic Roles and Molecular Targeting of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, June 2013. http://dx.doi.org/10.21236/ada613869.

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Zhang, Kezhong. Endoplasmic Reticulum-Associated Degradation Factor ERLIN2: Oncogenic Roles and Molecular Targeting of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, June 2012. http://dx.doi.org/10.21236/ada603934.

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