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hsp70 interacting protein

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https://www.readbyqxmd.com/read/29147715/the-impact-of-ultraviolet-b-uv-b-radiation-in-combination-with-different-temperatures-in-the-early-life-stage-of-zebrafish-danio-rerio
#1
Feyza Icoglu Aksakal, Abdulkadir Ciltas
Ultraviolet B (UV-B) radiation is an environmental stressor with detrimental effects on many aquatic organisms including fish. In addition, UV-B exposure combined with other environmental factors could have even more negative effects. The purpose of this study was to investigate the effect of UV-B radiation exposure on zebrafish embryos/larvae in terms of survival, developmental toxicity and the mRNA levels of the genes related to oxidative stress and innate immune response at different temperatures (24 °C, 28 °C and 30 °C)...
November 17, 2017: Photochemical & Photobiological Sciences
https://www.readbyqxmd.com/read/29145196/aqp2-abundance-is-regulated-by-the-e3-ligase-chip-via-hsp70
#2
Mariangela Centrone, Marianna Ranieri, Annarita Di Mise, Sante Princiero Berlingerio, Annamaria Russo, Peter M T Deen, Olivier Staub, Giovanna Valenti, Grazia Tamma
BACKGROUND/AIMS: AQP2 expression is mainly controlled by vasopressin-dependent changes in protein abundance which is in turn regulated by AQP2 ubiquitylation and degradation, however the proteins involved in these processes are largely unknown. Here, we investigated the potential role of the CHIP E3 ligase in AQP2 regulation. METHODS: MCD4 cells and kidney slices were used to study the involvement of the E3 ligase CHIP on AQP2 protein abundance by cell homogenization and immunoprecipitation followed by immunoblotting...
November 17, 2017: Cellular Physiology and Biochemistry
https://www.readbyqxmd.com/read/29140163/hsp70s-enhance-a-phytophthora-infestans-effector-induced-cell-death-via-a-mapk-cascade-in-nicotiana-benthamiana
#3
Joohyun Lee, So Eui Lee, SooHyun Oh, Eunyoung Seo, Doil Choi
A destructive pathogen, Phytophthora infestans, secretes hundreds of effectors for successful survival in its host plants. The effectors modulate plant defense system at diverse cellular compartments to take an advantage of pathogen survivals. There were a few researches shown the mode-of-action of each effectors and their interacting proteins in plant cells. Here, we investigated the mode-of-action of a P. infestans effector, Pi23226, which induces cell death in Nicotiana benthamiana. To identify its host factors, we performed co-immunoprecipitation and liquid chromatography-mass spectrometry, and selected members of HSP70 as candidates...
November 15, 2017: Molecular Plant-microbe Interactions: MPMI
https://www.readbyqxmd.com/read/29128340/the-interaction-between-a-hsp-70-gene-variant-with-dietary-calories-in-determining-serum-markers-of-inflammation-and-cardiovascular-risk
#4
Mehrane Mehramiz, Seyed Mahdi Hassanian, Maryam Mardan-Nik, Alireza Pasdar, Khadijeh Jamialahmadi, Hamid Fiuji, Mehrdad Moetamani-Ahmadi, Seyed Mohammad Reza Parizadeh, Mohsen Moohebati, Alireza Heidari-Bakavoli, Mahmoud Ebrahimi, Gordon A Ferns, Majid Ghayour-Mobarhan, Amir Avan
BACKGROUND: The high prevalence of cardiovascular disease (CVD) globally is attributable to an interaction between environmental and genetic factors. Gene × diet interaction studies aim to explore how a modifiable factor interacts with genetic predispositions. Here we have explored the interaction of a heat shock protein (HSP70) gene polymorphism (+1267A > G) with dietary intake and their possible association with serum C-reactive protein (CRP), an inflammatory marker, that is a major component of CVD risk...
October 24, 2017: Clinical Nutrition: Official Journal of the European Society of Parenteral and Enteral Nutrition
https://www.readbyqxmd.com/read/29124426/molecular-chaperones-involved-in-mitochondrial-iron-sulfur-protein-biogenesis
#5
REVIEW
Rafal Dutkiewicz, Malgorzata Nowak
Iron-sulfur (FeS) clusters are prosthetic groups critical for the function of many proteins in all domains of life. FeS proteins function in processes ranging from oxidative phosphorylation and cofactor biosyntheses to DNA/RNA metabolism and regulation of gene expression. In eukaryotic cells, mitochondria play a central role in the process of FeS biogenesis and support maturation of FeS proteins localized within mitochondria and in other cellular compartments. In humans, defects in mitochondrial FeS cluster biogenesis lead to numerous pathologies, which are often fatal...
November 9, 2017: Journal of Biological Inorganic Chemistry: JBIC
https://www.readbyqxmd.com/read/29124308/the-%C3%AE-6-%C3%AE-7-region-of-the-hsp70-substrate-binding-domain-mediates-heat-shock-response-and-prion-propagation
#6
Linan Xu, Weibin Gong, Sarah A Cusack, Huiwen Wu, Harriët M Loovers, Hong Zhang, Sarah Perrett, Gary W Jones
Hsp70 is a highly conserved chaperone that in addition to providing essential cellular functions and aiding in cell survival following exposure to a variety of stresses is also a key modulator of prion propagation. Hsp70 is composed of a nucleotide-binding domain (NBD) and substrate-binding domain (SBD). The key functions of Hsp70 are tightly regulated through an allosteric communication network that coordinates ATPase activity with substrate-binding activity. How Hsp70 conformational changes relate to functional change that results in heat shock and prion-related phenotypes is poorly understood...
November 9, 2017: Cellular and Molecular Life Sciences: CMLS
https://www.readbyqxmd.com/read/29107085/hsp70-participates-in-pink1-mediated-mitophagy-by-regulating-the-stability-of-pink1
#7
Qian Zheng, Chuxin Huang, Jifeng Guo, Jieqiong Tan, Chunyu Wang, Beisha Tang, Hainan Zhang
INTRODUCTION: Loss-of function mutations in PTEN-induced putative kinase 1 (PINK1) is one of the most common causes of autosomal recessive Parkinson's disease (PD). PINK1-mediated mitophagy is critical to mitochondrial quality control and plays an important role in PD pathogenesis. Therefore, identifying the regulatory mechanisms of PINK1 expression may provide novel opportunities for PD therapy. Heat-shock protein 70kDa (Hsp70) is involved in neuroprotection as a molecular chaperone in neurodegenerative disorders such as PD...
October 28, 2017: Neuroscience Letters
https://www.readbyqxmd.com/read/29095844/ensemble-based-modeling-and-rigidity-decomposition-of-allosteric-interaction-networks-and-communication-pathways-in-cyclin-dependent-kinases-differentiating-kinase-clients-of-the-hsp90-cdc37-chaperone
#8
Gabrielle Stetz, Amanda Tse, Gennady M Verkhivker
The overarching goal of delineating molecular principles underlying differentiation of protein kinase clients and chaperone-based modulation of kinase activity is fundamental to understanding activity of many oncogenic kinases that require chaperoning of Hsp70 and Hsp90 systems to attain a functionally competent active form. Despite structural similarities and common activation mechanisms shared by cyclin-dependent kinase (CDK) proteins, members of this family can exhibit vastly different chaperone preferences...
2017: PloS One
https://www.readbyqxmd.com/read/29094278/substrates-of-the-chloroplast-small-heat-shock-proteins-22e-f-point-to-thermolability-as-a-regulative-switch-for-heat-acclimation-in-chlamydomonas-reinhardtii
#9
Mark Rütgers, Ligia Segatto Muranaka, Timo Mühlhaus, Frederik Sommer, Sylvia Thoms, Juliane Schurig, Felix Willmund, Miriam Schulz-Raffelt, Michael Schroda
We have identified 39 proteins that interact directly or indirectly with high confidence with chloroplast HSP22E/F under heat stress thus revealing chloroplast processes affected by heat. Under conditions promoting protein unfolding, small heat shock proteins (sHsps) prevent the irreversible aggregation of unfolding proteins by integrating into forming aggregates. Aggregates containing sHsps facilitate the access of Hsp70 and ClpB/Hsp104 chaperones, which in ATP-dependent reactions disentangle individual proteins from the aggregates and assist in their refolding to the native state...
November 1, 2017: Plant Molecular Biology
https://www.readbyqxmd.com/read/29091030/chip-as-a-membrane-shuttling-proteostasis-sensor
#10
Yannick Kopp, Wei-Han Lang, Tobias B Schuster, Adrián Martínez-Limón, Harald F Hofbauer, Robert Ernst, Giulia Calloni, R Martin Vabulas
Cells respond to protein misfolding and aggregation in the cytosol by adjusting gene transcription and a number of post-transcriptional processes. In parallel to functional reactions, cellular structure changes as well; however, the mechanisms underlying the early adaptation of cellular compartments to cytosolic protein misfolding are less clear. Here we show that the mammalian ubiquitin ligase C-terminal Hsp70-interacting protein (CHIP), if freed from chaperones during acute stress, can dock on cellular membranes thus performing a proteostasis sensor function...
November 1, 2017: ELife
https://www.readbyqxmd.com/read/29089903/intravesicular-phosphatase-phospho1-function-in-enamel-mineralization-and-prism-formation
#11
Mirali Pandya, Lauren Rosene, Colin Farquharson, José L Millán, Thomas G H Diekwisch
The transport of mineral ions from the enamel organ-associated blood vessels to the developing enamel crystals involves complex cargo packaging and carriage mechanisms across several cell layers, including the ameloblast layer and the stratum intermedium. Previous studies have established PHOSPHO1 as a matrix vesicle membrane-associated phosphatase that interacts with matrix vesicles molecules phosphoethanolamine and phosphocholine to initiate apatite crystal formation inside of matrix vesicles in bone. In the present study, we sought to determine the function of Phospho1 during amelogenesis...
2017: Frontiers in Physiology
https://www.readbyqxmd.com/read/29084221/broadening-the-functionality-of-a-j-protein-hsp70-molecular-chaperone-system
#12
Brenda A Schilke, Szymon J Ciesielski, Thomas Ziegelhoffer, Erina Kamiya, Marco Tonelli, Woonghee Lee, Gabriel Cornilescu, Justin K Hines, John L Markley, Elizabeth A Craig
By binding to a multitude of polypeptide substrates, Hsp70-based molecular chaperone systems perform a range of cellular functions. All J-protein co-chaperones play the essential role, via action of their J-domains, of stimulating the ATPase activity of Hsp70, thereby stabilizing its interaction with substrate. In addition, J-proteins drive the functional diversity of Hsp70 chaperone systems through action of regions outside their J-domains. Targeting to specific locations within a cellular compartment and binding of specific substrates for delivery to Hsp70 have been identified as modes of J-protein specialization...
October 2017: PLoS Genetics
https://www.readbyqxmd.com/read/29083508/innate-immunity-protein-tag7-pgrp-s-activates-lymphocytes-capable-of-fasl-fas-dependent-contact-killing-of-virus-infected-cells
#13
Tatiana N Sharapova, Olga K Ivanova, Vladimir S Prasolov, Elena A Romanova, Lidia P Sashchenko, Denis V Yashin
The innate immunity protein Tag7 (PGRP-S, PGLYRP1) is involved in antimicrobial and antitumor defense. As shown in our previous studies, Tag7 specifically interacts with the major heat shock protein Hsp70 to form a stable Tag7-Hsp70 complex with cytotoxic activity against tumor cells. A stable complex of Tag7 with the calcium-binding protein Mts1 (S100A4) stimulates migration of lymphocytes. Moreover, Tag7 can activate cytotoxic lymphocytes that recognize and kill HLA-negative tumor cells. Here, we have shown that Tag 7 treatment of human peripheral blood mononuclear cells (PBMCs) results in activation of different cytotoxic lymphocyte populations-natural killer (NK) cells and CD8(+) NKG2D(+) T lymphocytes-that kill Moloney murine leukemia virus (MMLV) infected SC-1 cells using different mechanisms of cell death induction...
October 30, 2017: IUBMB Life
https://www.readbyqxmd.com/read/29075633/structure-and-interactions-of-the-tpr-domain-of-sgt2-with-yeast-chaperones-and-ybr137wp
#14
Ewelina M Krysztofinska, Nicola J Evans, Arjun Thapaliya, James W Murray, Rhodri M L Morgan, Santiago Martinez-Lumbreras, Rivka L Isaacson
Small glutamine-rich tetratricopeptide repeat-containing protein 2 (Sgt2) is a multi-module co-chaperone involved in several protein quality control pathways. The TPR domain of Sgt2 and several other proteins, including SGTA, Hop, and CHIP, is a highly conserved motif known to form transient complexes with molecular chaperones such as Hsp70 and Hsp90. In this work, we present the first high resolution crystal structures of Sgt2_TPR alone and in complex with a C-terminal peptide PTVEEVD from heat shock protein, Ssa1...
2017: Frontiers in Molecular Biosciences
https://www.readbyqxmd.com/read/29069650/dnajb1-hsp40-suppresses-melanoma-differentiation-associated-gene-5-mitochondrial-antiviral-signaling-protein-function-in-conjunction-with-hsp70
#15
Ken Takashima, Hiroyuki Oshiumi, Misako Matsumoto, Tsukasa Seya
Melanoma differentiation-associated gene 5 (MDA5) is a pattern recognition receptor that recognizes cytoplasmic viral double-stranded RNA (dsRNA) and initiates rapid innate antiviral responses. MDA5 forms a filament-like multimer along the dsRNA leading to oligomerization, which in turn activates the adaptor protein mitochondrial antiviral signaling protein (MAVS) to provide a signal platform for the induction of type I interferon (IFN) and proinflammatory cytokines. The conformational switch of MDA5 causes antiviral defense, but excessive activation of the MDA5-MAVS pathway may result in autoimmune diseases...
October 26, 2017: Journal of Innate Immunity
https://www.readbyqxmd.com/read/29069432/sumo-e3-ligase-slsiz1-facilitates-heat-tolerance-in-tomato
#16
Song Zhang, Shiju Wang, Jinlian Lv, Zhuangbin Liu, Yong Wang, Nana Ma, Qingwei Meng
High temperature has become a major abiotic stress that limits crop productivity. Heat shock transcription factors (HSFs) and heat shock proteins (HSPs) play important roles in enhancing thermotolerance of plants. SUMOylation is an important post-translational modification in regulating cellular functions in eukaryotes. SIZ1, a well-characterized SUMO E3 ligase, mediates process of SUMOylation. In this study, SUMO conjugations were clearly induced by high temperature. Overexpression of SIZ1 SUMO E3 ligase (SlSIZ1) in tomato could enhance the tolerance to heat stress in tomato...
October 24, 2017: Plant & Cell Physiology
https://www.readbyqxmd.com/read/29064368/ampylation-targets-the-rate-limiting-step-of-bip-s-atpase-cycle-for-its-functional-inactivation
#17
Steffen Preissler, Lukas Rohland, Yahui Yan, Ruming Chen, Randy J Read, David Ron
The endoplasmic reticulum (ER)-localized Hsp70 chaperone BiP contributes to protein folding homeostasis by engaging unfolded client proteins in a process that is tightly coupled to ATP binding and hydrolysis. The inverse correlation between BiP AMPylation and the burden of unfolded ER proteins suggests a post-translational mechanism for adjusting BiP's activity to changing levels of ER stress, but the underlying molecular details are unexplored. We present biochemical and crystallographic studies indicating that irrespective of the identity of the bound nucleotide AMPylation biases BiP towards a conformation normally attained by the ATP-bound chaperone...
October 24, 2017: ELife
https://www.readbyqxmd.com/read/29063205/steered-molecular-dynamics-simulation-of-the-binding-of-the-bovine-auxilin-j-domain-to-the-hsc70-nucleotide-binding-domain
#18
You-Lin Xue, Lei Zhou, Yuna Sun, Hui Li, Gary W Jones, Youtao Song
The Hsp70 and Hsp40 chaperone machine plays critical roles in protein folding, membrane translocation, and protein degradation by binding and releasing protein substrates in a process that utilizes ATP. The activities of the Hsp70 family of chaperones are recruited and stimulated by the J domains of Hsp40 chaperones. However, structural information on the Hsp40-Hsp70 complex is lacking, and the molecular details of this interaction are yet to be elucidated. Here we used steered molecular dynamics (SMD) simulations to investigate the molecular interactions that occur during the dissociation of the auxilin J domain from the Hsc70 nucleotide-binding domain (NBD)...
October 23, 2017: Journal of Molecular Modeling
https://www.readbyqxmd.com/read/29059239/co-opting-atp-generating-glycolytic-enzyme-pgk1-phosphoglycerate-kinase-facilitates-the-assembly-of-viral-replicase-complexes
#19
K Reddisiva Prasanth, Chingkai Chuang, Peter D Nagy
The intricate interactions between viruses and hosts include exploitation of host cells for viral replication by using many cellular resources, metabolites and energy. Tomato bushy stunt virus (TBSV), similar to other (+)RNA viruses, induces major changes in infected cells that lead to the formation of large replication compartments consisting of aggregated peroxisomal and ER membranes. Yet, it is not known how TBSV obtains the energy to fuel these energy-consuming processes. In the current work, the authors discovered that TBSV co-opts the glycolytic ATP-generating Pgk1 phosphoglycerate kinase to facilitate the assembly of new viral replicase complexes...
October 2017: PLoS Pathogens
https://www.readbyqxmd.com/read/29051186/distinct-roles-of-intracellular-heat-shock-protein-70-hsp70-in-maintaining-gastrointestinal-homeostasis
#20
Yunwei Wang, Fanfei Lin, Xiaorong Zhu, Vanessa A Leone, Sushila R Dalal, Yun Tao, Jeannette S Messer, Eugene B Chang
The inducible heat shock protein 70 (Hsp70) is both cytoprotective and immunomodulatory, potentially accounting for its critical role in maintaining gastrointestinal homeostasis. When levels are reduced in conditions like inflammatory bowel diseases (IBD), loss of function contributes to the severity and chronicity of these diseases, although through which cell types and mechanisms remains unclear. Here, the role of Hsp70-mediated intestinal epithelial protection and immune regulation in experimental colitis was examined by using a villin-promoter driven Hsp70 transgene in the TNBS and DSS models and in IL10/Hsp70 double knockout (IL10(-/-)/Hsp70(-/-)) mice...
October 19, 2017: American Journal of Physiology. Gastrointestinal and Liver Physiology
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