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hsp70 interacting protein

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https://www.readbyqxmd.com/read/28095400/computational-analysis-of-residue-interaction-networks-and-coevolutionary-relationships-in-the-hsp70-chaperones-a-community-hopping-model-of-allosteric-regulation-and-communication
#1
Gabrielle Stetz, Gennady M Verkhivker
Allosteric interactions in the Hsp70 proteins are linked with their regulatory mechanisms and cellular functions. Despite significant progress in structural and functional characterization of the Hsp70 proteins fundamental questions concerning modularity of the allosteric interaction networks and hierarchy of signaling pathways in the Hsp70 chaperones remained largely unexplored and poorly understood. In this work, we proposed an integrated computational strategy that combined atomistic and coarse-grained simulations with coevolutionary analysis and network modeling of the residue interactions...
January 2017: PLoS Computational Biology
https://www.readbyqxmd.com/read/28079882/stability-of-the-cancer-target-ddias-is-regulated-by-the-chip-hsp70-pathway-in-lung-cancer-cells
#2
Kyoung-Jae Won, Joo-Young Im, Bo-Kyung Kim, Hyun Seung Ban, Young-Jin Jung, Kyeong Eun Jung, Misun Won
DNA damage-induced apoptosis suppressor (DDIAS) rescues lung cancer cells from apoptosis in response to DNA damage. DDIAS is transcriptionally activated by NFATc1 and EGF-mediated ERK5/MEF2B, leading to cisplatin resistance and cell invasion. Therefore, DDIAS is suggested as a therapeutic target for lung cancer. Here, we report that DDIAS stability is regulated by E3 U-box ubiquitin ligase carboxyl terminus of HSP70-interacting protein (CHIP)-mediated proteasomal degradation. We first isolated CHIP as an interacting partner of DDIAS by yeast two-hybrid screening...
January 12, 2017: Cell Death & Disease
https://www.readbyqxmd.com/read/28073608/design-synthesis-and-biological-evaluation-of-7-aryl-2-3-dihydro-1-4-dioxino-2-3-g-quinoline-derivatives-as-potential-hsp90-inhibitors-and-anticancer-agents
#3
Sina Omid Malayeri, Khalil Abnous, Atefeh Arab, Maryam Akaberi, Soghra Mehri, Afshin Zarghi, Razieh Ghodsi
A new series of quinoline analogues was designed and synthesized as Hsp90 inhibitors. The cytotoxic activity of the synthesized compounds was evaluated against three human cancer cell lines including MCF-7 (human breast cancer cells), DU145 (human prostate cancer cell lines), and A549 (adenocarcinomic human alveolar basal epithelial cells). Some of our compounds (13a-13f) showed significant cytotoxic activity on MCF-7 cells. The most potent anti-proliferative compounds were also tested against Her2, a client protein of Hsp90...
January 2, 2017: Bioorganic & Medicinal Chemistry
https://www.readbyqxmd.com/read/28067917/structural-insights-into-a-unique-hsp70-hsp40-interaction-in-the-eukaryotic-ribosome-associated-complex
#4
Felix Alexander Weyer, Andrea Gumiero, Genís Valentín Gesé, Karine Lapouge, Irmgard Sinning
Cotranslational chaperones assist de novo folding of nascent polypeptides, prevent them from aggregating and modulate translation. The ribosome-associated complex (RAC) is unique in that the Hsp40 protein Zuo1 and the atypical Hsp70 chaperone Ssz1 form a stable heterodimer, which acts as a cochaperone for the Hsp70 chaperone Ssb. Here we present the structure of the Chaetomium thermophilum RAC core comprising Ssz1 and the Zuo1 N terminus. We show how the conserved allostery of Hsp70 proteins is abolished and this Hsp70-Hsp40 pair is molded into a functional unit...
January 9, 2017: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/28053106/grp78-is-an-important-host-factor-for-japanese-encephalitis-virus-entry-and-replication-in-mammalian-cells
#5
Minu Nain, Sriparna Mukherjee, Sonali Porey Karmakar, Adrienne W Paton, James C Paton, M Z Abdin, Anirban Basu, Manjula Kalia, Sudhanshu Vrati
: Japanese encephalitis virus (JEV), a mosquito-borne flavivirus, is the leading cause of viral encephalitis in South-East Asia with potential to become a global pathogen. Here we identify the Glucose regulated protein 78 (GRP78) as an important host protein for virus entry and replication. Using the plasma membrane fractions from mouse neuronal (Neuro2a) cells, mass spectroscopy analysis identified GRP78 as a protein interacting with recombinant JEV envelope protein domain III. GRP78 was found to express on the plasma membrane of Neuro2a, mouse primary neurons, and human epithelial Huh-7 cells...
January 4, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28053100/heat-shock-protein-90-ensures-efficient-mumps-virus-replication-by-assisting-with-viral-polymerase-complex-formation
#6
Hiroshi Katoh, Toru Kubota, Yuichiro Nakatsu, Maino Tahara, Minoru Kidokoro, Makoto Takeda
: Paramyxoviral RNAs are synthesized by a viral RNA-dependent RNA polymerase (RdRp) consisting of the large (L) protein and its cofactor phosphoprotein (P protein). The L protein is a multifunctional protein that catalyzes RNA synthesis, mRNA capping and mRNA polyadenylation. Growing evidence shows that the stability of several paramyxovirus L proteins is regulated by heat shock protein 90 (Hsp90). In this study, we demonstrated that Hsp90 activity was important for mumps virus (MuV) replication...
January 4, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28042827/bag2-interferes-with-chip-mediated-ubiquitination-of-hsp72
#7
Bianca Schönbühler, Verena Schmitt, Heike Huesmann, Andreas Kern, Martin Gamerdinger, Christian Behl
The maintenance of cellular proteostasis is dependent on molecular chaperones and protein degradation pathways. Chaperones facilitate protein folding, maturation, and degradation, and the particular fate of a misfolded protein is determined by the interaction of chaperones with co-chaperones. The co-factor CHIP (C-terminus of HSP70-inteacting protein, STUB1) ubiquitinates chaperone substrates and directs proteins to the cellular degradation systems. The activity of CHIP is regulated by two co-chaperones, BAG2 and HSPBP1, which are potent inhibitors of the E3 ubiquitin ligase activity...
December 30, 2016: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/28035761/analysis-of-swi-formation-and-propagation-events
#8
Zhiqiang Du, Dustin Kenneth Goncharoff, Xudong Cheng, Liming Li
The budding yeast, Saccharomyces cerevisiae, harbors several prions that are transmitted as altered, heritable protein conformations. [SWI(+) ] is one such prion whose determinant is Swi1, a subunit of the evolutionarily conserved chromatin-remodeling complex SWI/SNF. Despite the importance of Swi1, the molecular events that lead to [SWI(+) ] prionogenesis remain poorly understood. In this study, we have constructed floccullin-promoter-based URA3 reporters for [SWI(+) ] identification. Using these reporters, we show that the spontaneous formation frequency of [SWI(+) ] is significantly higher than that of [PSI(+) ] (prion form of Sup35)...
December 30, 2016: Molecular Microbiology
https://www.readbyqxmd.com/read/28031489/unrestrained-ampylation-targets-cytosolic-chaperones-and-activates-the-heat-shock-response
#9
Matthias C Truttmann, Xu Zheng, Leo Hanke, Jadyn R Damon, Monique Grootveld, Joanna Krakowiak, David Pincus, Hidde L Ploegh
Protein AMPylation is a conserved posttranslational modification with emerging roles in endoplasmic reticulum homeostasis. However, the range of substrates and cell biological consequences of AMPylation remain poorly defined. We expressed human and Caenorhabditis elegans AMPylation enzymes-huntingtin yeast-interacting protein E (HYPE) and filamentation-induced by cyclic AMP (FIC)-1, respectively-in Saccharomyces cerevisiae, a eukaryote that lacks endogenous protein AMPylation. Expression of HYPE and FIC-1 in yeast induced a strong cytoplasmic Hsf1-mediated heat shock response, accompanied by attenuation of protein translation, massive protein aggregation, growth arrest, and lethality...
January 10, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28028182/domain-mapping-of-the-heat-shock-protein-70-reveals-that-glutamic-acid-446-and-arginine-447-are-critical-for-regulating-superoxide-dismutase-2-function
#10
Adeleye J Afolayan, Maxwell Alexander, Rebecca L Holme, Teresa Michalkiewicz, Ujala Rana, Ru-Jeng Teng, Sara Zemanovic, Daisy Sahoo, Kirkwood A Pritchard, Girija G Konduri
Stress-inducible heat shock protein 70 (hsp70) interacts with superoxide dismutase-2 (SOD2) in the cytosol after synthesis to transfer the enzyme to the mitochondria for subsequent activation. However, the structural basis for this interaction remains to be defined. To map the SOD2-binding site in hsp70, mutants of hsp70 were made and tested for their ability to bind SOD2. These studies showed that SOD2 binds in the amino acid 393-537 region of the chaperone. To map the hsp70-binding site in SOD2, we used a series of pulldown assays and showed that hsp70 binds to the amino-terminal domain of SOD2...
December 27, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28027486/differential-expression-of-the-nucleolar-protein-fibrillarin-during-mammalian-spermatogenesis-and-its-probable-association-with-chromatoid-body-components
#11
Larissa Fiamengui de Pauli, Elisa Gomes Santos, Fernanda Pazotti Daher Arcangelo, Wilson Aparecido Orcini, Rita Luiza Peruquetti
Chromatoid body (CB) is a cytoplasmic structure of male germ cells that has been indicated as having a role in the RNA and protein storage for the final differentiation of spermatozoa. Recent studies have indicated that some of these macromolecular complex components have nucleolar origin. The aims of the present study were to monitor the expression of fibrillarin nucleolar protein in mammalian seminiferous tubules at different stages of the spermatogenic cycle; to check fibrillarin distribution during the CB assembly; and also its interaction with two well-known CB markers (MIWI and HSP70)...
December 14, 2016: Micron: the International Research and Review Journal for Microscopy
https://www.readbyqxmd.com/read/28013030/interaction-of-e-coli-hsp90-with-dnak-involves-the-dnaj-binding-region-of-dnak
#12
Andrea N Kravats, Shannon M Doyle, Joel R Hoskins, Olivier Genest, Erin Doody, Sue Wickner
The 90-kDa heat shock protein (Hsp90) is a widely conserved and ubiquitous molecular chaperone that participates in ATP-dependent protein remodeling in both eukaryotes and prokaryotes. It functions in conjunction with Hsp70 and the Hsp70 cochaperones, an Hsp40 (J-protein) and a nucleotide exchange factor. In Escherichia coli, the functional collaboration between Hsp90Ec and Hsp70, DnaK, requires that the two chaperones directly interact. We used molecular docking to model the interaction of Hsp90Ec and DnaK...
December 21, 2016: Journal of Molecular Biology
https://www.readbyqxmd.com/read/28000699/absence-of-hikeshi-a-nuclear-transporter-for-heat-shock-protein-hsp70-causes-infantile-hypomyelinating-leukoencephalopathy
#13
Catalina Vasilescu, Pirjo Isohanni, Maarit Palomäki, Helena Pihko, Anu Suomalainen, Christopher J Carroll
Genetic leukoencephalopathies are a heterogeneous group of central nervous system disorders with white matter involvement. In a Finnish patient, we identified a novel homozygous disease-causing variant in HIKESHI, c.11G>C, p.(Cys4Ser), leading to hypomyelinating leukoencephalopathy with periventricular cysts and vermian atrophy. A founder Ashkenazi-Jewish disease-causing variant recently linked Hikeshi and its heat-shock protective function to leukoencephalopathy. In our patient, clinical features of lower limb spasticity, optic atrophy, nystagmus, and severe developmental delay were similar to reported patients...
December 21, 2016: European Journal of Human Genetics: EJHG
https://www.readbyqxmd.com/read/27975204/a-disulfide-bonded-dnak-dimer-is-maintained-in-an-atp-bound-state
#14
Qingdai Liu, Hongtao Li, Ying Yang, Xueli Tian, Jiayue Su, Lei Zhou, Qinglian Liu
DnaK, a major Hsp70 molecular chaperones in Escherichia coli, is a widely used model for studying Hsp70s. We recently solved a crystal structure of DnaK in complex with ATP and showed that DnaK was packed as a dimer in the crystal structure. Our previous biochemical studies supported the formation of a specific DnaK dimer as observed in the crystal structure in solution in the presence of ATP and suggested an important role of this dimer in efficient interaction with Hsp40 co-chaperones. In this study, we dissected the biochemical properties of this DnaK dimer...
December 14, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/27966061/ubl-bag-domain-co-chaperones-cause-cellular-stress-upon-overexpression-through-constitutive-activation-of-hsf1
#15
Esben G Poulsen, Caroline Kampmeyer, Franziska Kriegenburg, Jens V Johansen, Kay Hofmann, Christian Holmberg, Rasmus Hartmann-Petersen
As a result of exposure to stress conditions, mutations, or defects during synthesis, cellular proteins are prone to misfold. To cope with such partially denatured proteins, cells mount a regulated transcriptional response involving the Hsf1 transcription factor, which drives the synthesis of molecular chaperones and other stress-relieving proteins. Here, we show that the fission yeast Schizosaccharomyces pombe orthologues of human BAG-1, Bag101, and Bag102, are Hsp70 co-chaperones that associate with 26S proteasomes...
December 14, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/27941812/vrk3-mediated-nuclear-localization-of-hsp70-prevents-glutamate-excitotoxicity-induced-apoptosis-and-a%C3%AE-accumulation-via-enhancement-of-erk-phosphatase-vhr-activity
#16
Haengjin Song, Wanil Kim, Sung-Hoon Kim, Kyong-Tai Kim
Most of neurodegenerative disorders are associated with protein aggregation. Glutamate-induced excitotoxicity and persistent extracellular signal-regulated kinase (ERK) activation are also implicated in neurodegenerative diseases. Here, we found that vaccinia-related kinase 3 (VRK3) facilitates nuclear localization of glutamate-induced heat shock protein 70 (HSP70). Nuclear HSP70 leads to enhancement of vaccinia H1-related phosphatase (VHR) activity via protein-protein interaction rather than its molecular chaperone activity, thereby suppressing excessive ERK activation...
December 12, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27940052/lipopolysaccharide-and-heat-stress-impair-the-estradiol-biosynthesis-in-granulosa-cells-via-increase-of-hsp70-and-inhibition-of-smad3-phosphorylation-and-nuclear-translocation
#17
Hui Li, Shuangshuang Guo, Liuping Cai, Weiming Ma, Zhendan Shi
LPS and heat stress have been shown to exert various toxic effects in animals, as they induce estradiol biosynthesis dysfunction in granulosa cells (GCs) and result in low reproductive performance. However, there is limited information regarding their detailed mechanisms. In the present study, primary cultured porcine GCs were treated with LPS (1000ng/mL for 48h), or heat stress (41°C for 3h), in vitro, with or without the HSP70 inhibitor VER155008 (10μM), to investigate their potential mechanisms. To mimic the spike in HSP70 from LPS and heat stress, treatments with only the HSP70 activator STA-4783 (10μM for 3h or 48h) were also performed...
January 2017: Cellular Signalling
https://www.readbyqxmd.com/read/27917864/multivalent-contacts-of-the-hsp70-ssb-contribute-to-its-architecture-on-ribosomes-and-nascent-chain-interaction
#18
Marie A Hanebuth, Roman Kityk, Sandra J Fries, Alok Jain, Allison Kriel, Veronique Albanese, Tancred Frickey, Christine Peter, Matthias P Mayer, Judith Frydman, Elke Deuerling
Hsp70 chaperones assist de novo folding of newly synthesized proteins in all cells. In yeast, the specialized Hsp70 Ssb directly binds to ribosomes. The structural basis and functional mode of recruitment of Ssb to ribosomes is not understood. Here, we present the molecular details underlying ribosome binding of Ssb in Saccharomyces cerevisiae. This interaction is multifaceted, involving the co-chaperone RAC and two specific regions within Ssb characterized by positive charges. The C-terminus of Ssb mediates the key contact and a second attachment point is provided by a KRR-motif in the substrate binding domain...
December 5, 2016: Nature Communications
https://www.readbyqxmd.com/read/27903966/pde5-inhibitors-enhance-the-lethality-of-pemetrexed-through-inhibition-of-multiple-chaperone-proteins-and-via-the-actions-of-cyclic-gmp-and-nitric-oxide
#19
Laurence Booth, Jane L Roberts, Andrew Poklepovic, Sarah Gordon, Paul Dent
Phosphodiesterase 5 (PDE5) inhibitors prevent the breakdown of cGMP that results in prolonged protein kinase G activation and the generation of nitric oxide. PDE5 inhibitors enhanced the anti-NSCLC cell effects of the NSCLC therapeutic pemetrexed. [Pemetrexed + sildenafil] activated an eIF2α - ATF4 - CHOP - Beclin1 pathway causing formation of toxic autophagosomes; activated a protective IRE1 - XBP-1 - chaperone induction pathway; and activated a toxic eIF2α - CHOP - DR4 / DR5 / CD95 induction pathway. [Pemetrexed + sildenafil] reduced the expression of c-FLIP-s, MCL-1 and BCL-XL that was blocked in a cell-type -dependent fashion by either over-expression of HSP90 / GRP78 / HSP70 / HSP27 or by blockade of eIF2α-CHOP signaling...
November 26, 2016: Oncotarget
https://www.readbyqxmd.com/read/27901028/small-heat-shock-proteins-sequester-misfolding-proteins-in-near-native-conformation-for-cellular-protection-and-efficient-refolding
#20
Sophia Ungelenk, Fatemeh Moayed, Chi-Ting Ho, Tomas Grousl, Annette Scharf, Alireza Mashaghi, Sander Tans, Matthias P Mayer, Axel Mogk, Bernd Bukau
Small heat shock proteins (sHsp) constitute an evolutionary conserved yet diverse family of chaperones acting as first line of defence against proteotoxic stress. sHsps coaggregate with misfolded proteins but the molecular basis and functional implications of these interactions, as well as potential sHsp specific differences, are poorly explored. In a comparative analysis of the two yeast sHsps, Hsp26 and Hsp42, we show in vitro that model substrates retain near-native state and are kept physically separated when complexed with either sHsp, while being completely unfolded when aggregated without sHsps...
November 30, 2016: Nature Communications
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