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molecular chaperone and endoplasmic reticulum

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https://www.readbyqxmd.com/read/28190459/mutations-in-inpp5k-cause-a-form-of-congenital-muscular-dystrophy-overlapping-marinesco-sj%C3%A3-gren-syndrome-and-dystroglycanopathy
#1
Daniel P S Osborn, Heather L Pond, Neda Mazaheri, Jeremy Dejardin, Christopher J Munn, Khaloob Mushref, Edmund S Cauley, Isabella Moroni, Maria Barbara Pasanisi, Elizabeth A Sellars, R Sean Hill, Jennifer N Partlow, Rebecca K Willaert, Jaipreet Bharj, Reza Azizi Malamiri, Hamid Galehdari, Gholamreza Shariati, Reza Maroofian, Marina Mora, Laura E Swan, Thomas Voit, Francesco J Conti, Yalda Jamshidi, M Chiara Manzini
Congenital muscular dystrophies display a wide phenotypic and genetic heterogeneity. The combination of clinical, biochemical, and molecular genetic findings must be considered to obtain the precise diagnosis and provide appropriate genetic counselling. Here we report five individuals from four families presenting with variable clinical features including muscular dystrophy with a reduction in dystroglycan glycosylation, short stature, intellectual disability, and cataracts, overlapping both the dystroglycanopathies and Marinesco-Sjögren syndrome...
February 1, 2017: American Journal of Human Genetics
https://www.readbyqxmd.com/read/28167764/hy5-a-positive-regulator-of-light-signaling-negatively-controls-the-unfolded-protein-response-in-arabidopsis
#2
Ganesh M Nawkar, Chang Ho Kang, Punyakishore Maibam, Joung Hun Park, Young Jun Jung, Ho Byoung Chae, Yong Hun Chi, In Jung Jung, Woe Yeon Kim, Dae-Jin Yun, Sang Yeol Lee
Light influences essentially all aspects of plant growth and development. Integration of light signaling with different stress response results in improvement of plant survival rates in ever changing environmental conditions. Diverse environmental stresses affect the protein-folding capacity of the endoplasmic reticulum (ER), thus evoking ER stress in plants. Consequently, the unfolded protein response (UPR), in which a set of molecular chaperones is expressed, is initiated in the ER to alleviate this stress...
February 6, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28112451/calreticulin-is-a-fine-tuning-molecule-in-epibrassinolide-induced-apoptosis-through-activating-endoplasmic-reticulum-stress-in-colon-cancer-cells
#3
Pinar Obakan-Yerlikaya, Elif Damla Arisan, Ajda Coker-Gurkan, Kaan Adacan, Utku Özbey, Berna Somuncu, Didem Baran, Narçin Palavan-Ünsal
Epibrassinolide (EBR), a member of brassinostreoids plant hormones with cell proliferation promoting role in plants, is a natural polyhydroxysteroid with structural similarity to steroid hormones of vertebrates. EBR has antiproliferative and apoptosis-inducing effect in various cancer cells. Although EBR has been shown to affect survival and mitochondria-mediated apoptosis pathways in a p53-independent manner, the exact molecular targets of EBR are still under investigation. Our recent SILAC (Stable Isotope Labeling by Amino Acids in Cell Culture) data showed that the most significantly altered protein after EBR treatment was calreticulin (CALR)...
January 23, 2017: Molecular Carcinogenesis
https://www.readbyqxmd.com/read/28079009/emerging-roles-of-calreticulin-in-cancer-implications-for-therapy
#4
Kavya Venkateswaran, Amit Verma, Anant Narayan Bhatt, Anju Shrivastava, Kailash Manda, Hanumantharao G Raj, Ashok Prasad, Christophe Len, Virinder S Parmar, Bilikere Dwarakanath
Calreticulin (CRT), initially identified as a ubiquitous calcium-binding protein in the endoplasmic reticulum, has emerged as a multifunctional protein with roles in calcium homeostasis, molecular chaperoning and cell adhesion. Emerging evidence suggests its involvement in tumorigenesis facilitating proliferation, migration, and adhesion. CRT translocated to the cell surface (ecto-CRT) serves as a phagocytic signal for immunogenic cell death (ICD) mediated through dendritic cells (DCs) and cytotoxic T-cell activation thereby making tumors susceptible to immunotherapy-based anti-cancer strategies...
11, 2017: Current Protein & Peptide Science
https://www.readbyqxmd.com/read/28069662/endoplasmic-reticulum-stress-inhibition-limits-the-progression-of-chronic-kidney-disease-in-the-dahl-salt-sensitive-rat
#5
Victoria Yum, Rachel E Carlisle, Chao Lu, Elise Brimble, Jasmine Chahal, Chandak Upagupta, Kjetil Ask, Jeffrey G Dickhout
Proteinuria is one of the primary risk factors for the progression of chronic kidney disease (CKD) and has been implicated in the induction of endoplasmic reticulum (ER) stress. We hypothesized that the suppression of ER stress with a low molecular weight chemical chaperone, 4-phenylbutyric acid (4-PBA), would reduce the severity of CKD and proteinuria in the Dahl salt-sensitive (SS) hypertensive rat. To induce hypertension and CKD, 12-wk-old male rats were placed on a high-salt (HS) diet for 4 wk with or without 4-PBA treatment...
January 1, 2017: American Journal of Physiology. Renal Physiology
https://www.readbyqxmd.com/read/28032645/arabidopsis-b-cell-lymphoma2-bcl-2-associated-athanogene-7-bag7-mediated-heat-tolerance-requires-translocation-sumoylation-and-binding-to-wrky29
#6
Yurong Li, Brett Williams, Martin Dickman
To cope with stress and increased accumulation of misfolded proteins, plants and animals use a survival pathway known as the unfolded protein response (UPR) that signals between the endoplasmic reticulum (ER) and the nucleus to maintain cell homeostasis via proper folding of proteins. B-cell lymphoma2 (Bcl-2)-associated athanogene (BAG) proteins are an evolutionarily conserved family of co-chaperones that are linked to disease states in mammals and responses to environmental stimuli (biotic and abiotic) in plants...
December 29, 2016: New Phytologist
https://www.readbyqxmd.com/read/28028229/achromatopsia-mutations-target-sequential-steps-of-atf6-activation
#7
Wei-Chieh Chiang, Priscilla Chan, Bernd Wissinger, Ajoy Vincent, Anna Skorczyk-Werner, Maciej R Krawczyński, Randal J Kaufman, Stephen H Tsang, Elise Héon, Susanne Kohl, Jonathan H Lin
Achromatopsia is an autosomal recessive disorder characterized by cone photoreceptor dysfunction. We recently identified activating transcription factor 6 (ATF6) as a genetic cause of achromatopsia. ATF6 is a key regulator of the unfolded protein response. In response to endoplasmic reticulum (ER) stress, ATF6 migrates from the ER to Golgi to undergo regulated intramembrane proteolysis to release a cytosolic domain containing a basic leucine zipper (bZIP) transcriptional activator. The cleaved ATF6 fragment migrates to the nucleus to transcriptionally up-regulate protein-folding enzymes and chaperones...
January 10, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28028074/chaperone-driven-degradation-of-a-misfolded-proinsulin-mutant-in-parallel-with-restoration-of-wild-type-insulin-secretion
#8
Corey N Cunningham, Kaiyu He, Anoop Arunagiri, Adrienne W Paton, James C Paton, Peter Arvan, Billy Tsai
In heterozygous patients with a diabetic syndrome called Mutant INS-gene-induced Diabetes of Youth (MIDY), there is decreased insulin secretion when mutant proinsulin expression prevents wild type (WT) proinsulin from exiting the endoplasmic reticulum (ER), which is essential for insulin production. Our previous results revealed that mutant Akita proinsulin is triaged by ER-associated degradation (ERAD). We now find that the ER chaperone Grp170 participates in the degradation process by shifting Akita proinsulin from high molecular weight (MW) complexes towards smaller oligomeric species that are competent to undergo ERAD...
December 27, 2016: Diabetes
https://www.readbyqxmd.com/read/28012275/emc1-dependent-stabilization-drives-membrane-penetration-of-a-partially-destabilized-non-enveloped-virus
#9
Parikshit Bagchi, Takamasa Inoue, Billy Tsai
Destabilization of a non-enveloped virus generates a membrane transport-competent viral particle. Here we probe polyomavirus SV40 endoplasmic reticulum (ER)-to-cytosol membrane transport, a decisive infection step where destabilization initiates this non-enveloped virus for membrane penetration. We find that a member of the ER membrane protein complex (EMC) called EMC1 promotes SV40 ER membrane transport and infection. Surprisingly, EMC1 does so by using its predicted transmembrane residue D961 to bind to and stabilize the membrane-embedded partially destabilized SV40, thereby preventing premature viral disassembly...
December 24, 2016: ELife
https://www.readbyqxmd.com/read/27982123/unraveling-gene-expression-profiles-in-peripheral-motor-nerve-from-amyotrophic-lateral-sclerosis-patients-insights-into-pathogenesis
#10
Nilo Riva, Ferdinando Clarelli, Teuta Domi, Federica Cerri, Francesca Gallia, Amelia Trimarco, Paola Brambilla, Christian Lunetta, Alberto Lazzerini, Giuseppe Lauria, Carla Taveggia, Sandro Iannaccone, Eduardo Nobile-Orazio, Giancarlo Comi, Maurizio D'Antonio, Filippo Martinelli-Boneschi, Angelo Quattrini
The aim of the present study is to investigate the molecular pathways underlying amyotrophic lateral sclerosis (ALS) pathogenesis within the peripheral nervous system. We analyzed gene expression changes in human motor nerve diagnostic biopsies obtained from eight ALS patients and seven patients affected by motor neuropathy as controls. An integrated transcriptomics and system biology approach was employed. We identified alterations in the expression of 815 genes, with 529 up-regulated and 286 down-regulated in ALS patients...
December 16, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27928720/cardioprotection-of-exercise-preconditioning-involving-heat-shock-protein-70-and-concurrent-autophagy-a-potential-chaperone-assisted-selective-macroautophagy-effect
#11
Yang Yuan, Shan-Shan Pan, Yu-Jun Shen
It has been confirmed that exercise preconditioning (EP) has a protective effect on acute cardiovascular stress. However, how Hsp70 participates in EP-induced cardioprotection is unknown. EP may involve Hsp70 to repair unfolded proteins or may also stabilize the function of the endoplasmic reticulum via Hsp70-related autophagy to work on a protective formation. Our EP protocol involves four periods of 10 min running with 10 min recovery intervals. We added a period of exhaustive running to test this protective effect, using histology and molecular biotechnology methods to detect related markers...
December 7, 2016: Journal of Physiological Sciences: JPS
https://www.readbyqxmd.com/read/27925580/multiple-selection-filters-ensure-accurate-tail-anchored-membrane-protein-targeting
#12
Meera Rao, Voytek Okreglak, Un Seng Chio, Hyunju Cho, Peter Walter, Shu-Ou Shan
Accurate protein localization is crucial to generate and maintain organization in all cells. Achieving accuracy is challenging, as the molecular signals that dictate a protein's cellular destination are often promiscuous. A salient example is the targeting of an essential class of tail-anchored (TA) proteins, whose sole defining feature is a transmembrane domain near their C-terminus. Here we show that the Guided Entry of Tail-anchored protein (GET) pathway selects TA proteins destined to the endoplasmic reticulum (ER) utilizing distinct molecular steps, including differential binding by the co-chaperone Sgt2 and kinetic proofreading after ATP hydrolysis by the targeting factor Get3...
December 7, 2016: ELife
https://www.readbyqxmd.com/read/27917829/the-er-stress-sensor-perk-luminal-domain-functions-as-a-molecular-chaperone-to-interact-with-misfolded-proteins
#13
Peng Wang, Jingzhi Li, Bingdong Sha
PERK is one of the major sensor proteins which can detect the protein-folding imbalance generated by endoplasmic reticulum (ER) stress. It remains unclear how the sensor protein PERK is activated by ER stress. It has been demonstrated that the PERK luminal domain can recognize and selectively interact with misfolded proteins but not native proteins. Moreover, the PERK luminal domain may function as a molecular chaperone to directly bind to and suppress the aggregation of a number of misfolded model proteins...
December 1, 2016: Acta Crystallographica. Section D, Structural Biology
https://www.readbyqxmd.com/read/27916661/tetrameric-assembly-of-k-channels-requires-er-located-chaperone-proteins
#14
Kai Li, Qiang Jiang, Xue Bai, Yi-Feng Yang, Mei-Yu Ruan, Shi-Qing Cai
Tetrameric assembly of channel subunits in the endoplasmic reticulum (ER) is essential for surface expression and function of K(+) channels, but the molecular mechanism underlying this process remains unclear. In this study, we found through genetic screening that ER-located J-domain-containing chaperone proteins (J-proteins) are critical for the biogenesis and physiological function of ether-a-go-go-related gene (ERG) K(+) channels in both Caenorhabditis elegans and human cells. Human J-proteins DNAJB12 and DNAJB14 promoted tetrameric assembly of ERG (and Kv4...
January 5, 2017: Molecular Cell
https://www.readbyqxmd.com/read/27907150/molecular-characterization-of-two-monoclonal-antibodies-against-the-same-epitope-on-b-cell-receptor-associated-protein-31
#15
Won-Tae Kim, Saemina Shin, Hyo Jeong Hwang, Min Kyu Kim, Han-Sung Jung, Hwangseo Park, Chun Jeih Ryu
Previously, we showed that B-cell receptor associated protein 31 (BAP31), an endoplasmic reticulum (ER) membrane chaperone, is also expressed on the cell surface by two monoclonal antibodies (MAbs) 297-D4 and 144-A8. Both MAbs recognize the same linear epitope on the C-terminal domain of BAP31, although they were independently established. Here, flow cytometric analysis showed that 144-A8 had additional binding properties to some cells, as compared to 297-D4. Quantitative antigen binding assays also showed that 144-A8 had higher antigen binding capacity than 297-D4...
2016: PloS One
https://www.readbyqxmd.com/read/27903760/interactions-between-intersubunit-transmembrane-domains-regulate-the-chaperone-dependent-degradation-of-an-oligomeric-membrane-protein
#16
Teresa M Buck, Alexa S Jordahl, Megan E Yates, Mike Preston, Emily Cook, Thomas R Kleyman, Jeffrey L Brodsky
The Epithelial Sodium Channel (ENaC) in kidney regulates blood pressure through control of sodium and volume homeostasis, and in lung ENaC regulates the volume of airway and alveolar fluids.  ENaC is a heterotrimer of homologous α-, β-, and γ-subunits, and assembles in the Endoplasmic Reticulum (ER) before it traffics and functions at the plasma membrane. Improperly folded or orphaned ENaC subunits are subject to ER quality control and targeted for ER associated degradation (ERAD). We previously established that a conserved, ER lumenal, molecular chaperone, Lhs1/GRP170, selects αENaC, but not β- or γENaC, for degradation when the ENaC subunits were individually expressed...
November 30, 2016: Biochemical Journal
https://www.readbyqxmd.com/read/27869218/n-linked-glycosylation-at-asn152-on-cd147-affects-protein-folding-and-stability-promoting-tumour-metastasis-in-hepatocellular-carcinoma
#17
Jiang-Hua Li, Wan Huang, Peng Lin, Bo Wu, Zhi-Guang Fu, Hao-Miao Shen, Lin Jing, Zhen-Yu Liu, Yang Zhou, Yao Meng, Bao-Qing Xu, Zhi-Nan Chen, Jian-Li Jiang
Cluster of differentiation 147 (CD147), also known as extracellular matrix metalloproteinase inducer, is a transmembrane glycoprotein that mediates oncogenic processes partly through N-glycosylation modifications. N-glycosylation has been demonstrated to be instrumental for the regulation of CD147 function during malignant transformation. However, the role that site-specific glycosylation of CD147 plays in its defective function in hepatocellular carcinomacells needs to be determined. Here, we demonstrate that the modification of N-glycosylation at Asn152 on CD147 strongly promotes hepatocellular carcinoma (HCC) invasion and migration...
November 21, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27846717/-endoplasmic-reticulum-chaperones-at-the-tumor-cell-surface-and-in-the-extracellular-space
#18
V Brychtová, B Vojtěšek
BACKGROUND: Endoplasmic reticulum chaperones are stress induced proteins capable of translocation into cytosol, cell membrane or extracellular space. The chaperones are transported from the endoplasmic reticulum particularly under endoplasmic reticulum stress conditions, while their constitutive extracellular expression was found in many cancers. Cell surface or extracellular endoplasmic reticulum chaperones take up distinct functions compared to their endoplasmic reticulum resident variants because they act like multifunctional receptors and thus affect cell signaling and proliferation...
December 0: Klinická Onkologie: Casopis Ceské a Slovenské Onkologické Spolecnosti
https://www.readbyqxmd.com/read/27844183/evaluation-and-treatment-of-endoplasmic-reticulum-er-stress-in-right-ventricular-dysfunction-during-monocrotaline-induced-rat-pulmonary-arterial-hypertension
#19
Jing-Jing Wang, Xiang-Rong Zuo, Jian Xu, Jin-Yong Zhou, Hui Kong, Xiao-Ning Zeng, Wei-Ping Xie, Quan Cao
PURPOSE: Endoplasmic reticulum (ER) stress contributes to pulmonary artery hypertension (PAH). However, the exact roles of ER stress in right ventricular (RV) dysfunction, which is strongly associated with PAH, are largely unknown. Here, we aimed to explore how ER stress affects RV function in a rat PAH model and evaluated the effects of an ER stress inhibitor on RV dysfunction. METHODS: We examined expression changes of an ER marker: chaperone glucose-regulated protein 78 (GRP78), three ER stress sensor proteins: activating transcription factor 6 (ATF6), inositol-requiring enzyme 1 (IRE1), and protein kinase RNA-like endoplasmic reticulum kinase (PERK), and a key ER stress-induced apoptosis indicator: CCAAT/enhancer-binding protein homologous protein (CHOP), with inflammation indicators: interleukin 6 (IL-6), tumor necrosis factor-α (TNF-α), and matrix metalloproteinases (MMPs) in RV at 3, 7, 14 and 28 days following a single dose of monocrotaline (MCT) injection, with or without a preventive treatment [4-phenylbutyric acid (PBA)]...
December 2016: Cardiovascular Drugs and Therapy
https://www.readbyqxmd.com/read/27843443/rna-interference-mediated-simultaneous-suppression-of-seed-storage-proteins-in-rice-grains
#20
Kyoungwon Cho, Hye-Jung Lee, Yeong-Min Jo, Sun-Hyung Lim, Randeep Rakwal, Jong-Yeol Lee, Young-Mi Kim
Seed storage proteins (SSPs) such as glutelin, prolamin, and globulin are abundant components in some of the most widely consumed food cereals in the world. Synthesized in the rough endoplasmic reticulum (ER), SSPs are translocated to the protein bodies. Prolamins are located at the spherical protein body I derived from the ER, whereas, glutelins and globulin are accumulated in the irregularly shaped protein bodies derived from vacuoles. Our previous studies have shown that the individual suppression of glutelins, 13-kDa prolamins and globulin caused the compensative accumulation of other SSPs...
2016: Frontiers in Plant Science
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