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hsp70 interacting protein

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https://www.readbyqxmd.com/read/28205128/heat-shock-protein-70-protects-cardiomyocytes-through-suppressing-sumoylation-and-nucleus-translocation-of-phosphorylated-eukaryotic-elongation-factor-2-during-myocardial-ischemia-and-reperfusion
#1
Chao Zhang, Xiaojuan Liu, Jin Miao, Shengcun Wang, Liucheng Wu, Daliang Yan, Jingjing Li, Wanwan Guo, Xiang Wu, Aiguo Shen
Myocardial ischemia and reperfusion (MIR) results in cardiomyocyte apoptosis with severe outcomes, which blocks cardiac tissue recovering from myocardial ischemia diseases. Heat shock protein 70 (HSP70) is one of protective molecule chaperones which could regulate the nucleus translocation of other proteins. In addition, eukaryotic elongation factor 2 (eEF2), which modulates protein translation process, is vital to the recovery of heart during MIR. However, the relationship between HSP70 and eEF2 and its effects on MIR are unclear...
February 15, 2017: Apoptosis: An International Journal on Programmed Cell Death
https://www.readbyqxmd.com/read/28193840/co-chaperone-hsp70-hsp90-organizing-protein-hop-is-required-for-transposon-silencing-and-pirna-biogenesis
#2
Joseph A Karam, Rasesh Y Parikh, Dhananjaya Nayak, David Rosenkranz, Vamsi K Gangaraju
piRNAs are 26-30nt germ-line specific small non-coding RNAs that have evolutionarily conserved function in mobile genetic element (transposons) silencing and maintenance of genome integrity. Drosophila Hsp70/90 Organizing Protein Homolog (Hop), a co-chaperone, interacts with piRNA binding protein Piwi and mediates silencing of phenotypic variations. However, it is not known if Hop has a direct role in piRNA biogenesis and transposon silencing. Here, we show that knockdown of Hop in the germ-line nurse cells (GLKD) of Drosophila ovaries leads to activation of transposons...
February 13, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28182740/polymorphisms-of-heat-shock-protein-70-genes-hspa1a-hspa1b-and-hspa1l-and-susceptibility-of-noise-induced-hearing-loss-in-a-chinese-population-a-case-control-study
#3
Yanhong Li, Shanfa Yu, Guizhen Gu, Guoshun Chen, Yuxin Zheng, Jie Jiao, Wenhui Zhou, Hui Wu, Zengrui Zhang, Huanling Zhang, Lihua He, Qiuyue Yang, Xiangrong Xu
Noise-induced hearing loss (NIHL) is the second-most frequent form of sensorineural hearing loss. When exposed to the same noise, some workers develop NIHL while others do not, suggesting that NIHL may be associated with genetic factors. To explore the relationship between single nucleotide polymorphisms (SNPs) in heat shock protein 70 (HSP70) genes (HSPA1A, HSPA1B and HSPA1L) and susceptibility to NIHL in Han Chinese workers exposed to noise, a case-control association study was carried out with 286 hearing loss cases and 286 matched with gender, age, type of work, and exposure time, drawn from a population of 3790 noise-exposed workers...
2017: PloS One
https://www.readbyqxmd.com/read/28181153/an-interaction-study-in-mammalian-cells-demonstrates-weak-binding-of-hspb2-to-bag3-which-is-regulated-by-hspb3-and-abrogated-by-hspb8
#4
Federica F Morelli, Laura Mediani, Lonneke Heldens, Jessika Bertacchini, Ilaria Bigi, Arianna Dorotea Carrà, Jonathan Vinet, Serena Carra
The ten mammalian small heat shock proteins (sHSPs/HSPBs) show a different expression profile, although the majority of them are abundant in skeletal and cardiac muscles. HSPBs form hetero-oligomers and homo-oligomers by interacting together and complexes containing, e.g., HSPB2/HSPB3 or HSPB1/HSPB5 have been documented in mammalian cells and muscles. Moreover, HSPB8 associates with the Hsc70/Hsp70 co-chaperone BAG3, in mammalian, skeletal, and cardiac muscle cells. Interaction of HSPB8 with BAG3 regulates its stability and function...
February 8, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28155228/athop3-a-member-of-the-hop-family-in-arabidopsis-interacts-with-bip-and-plays-a-major-role-in-the-er-stress-response
#5
Nuria Fernández-Bautista, Lourdes Fernández-Calvino, Alfonso Muñoz, M Mar Castellano
HOP is a well-studied family of cytosolic cochaperones. However, the possible role of HOP during the ER stress response and their interactors within the ER were not previously addressed in any eukaryote. We have demonstrated that Arabidopsis HOP3, whose function was not studied before, interacts in vivo with cytosolic HSP90 and HSP70, and, unexpectedly, with BiP, a HSP70 ER-resident protein. Although BiP lacks the domain described in other eukaryotes for HOP-HSP70 binding, it interacts with HOP3 through a noncanonical association to its nucleotide binding domain...
February 2, 2017: Plant, Cell & Environment
https://www.readbyqxmd.com/read/28146421/the-hdac-inhibitor-ar42-interacts-with-pazopanib-to-kill-trametinib-dabrafenib-resistant-melanoma-cells-in-vitro-and-in-vivo
#6
Laurence Booth, Jane L Roberts, Cindy Sander, John Lee, John M Kirkwood, Andrew Poklepovic, Paul Dent
Studies focused on the killing of activated B-RAF melanoma cells by the histone deacetylase (HDAC) inhibitor AR42. Compared to other tumor cell lines, PDX melanoma isolates were significantly more sensitive to AR42-induced killing. AR42 and the multi-kinase inhibitor pazopanib interacted to activate: an eIF2α-Beclin1 pathway causing autophagosome formation; an eIF2α-DR4/DR5/CD95 pathway; and an eIF2α-dependent reduction in the expression of c-FLIP-s, MCL-1 and BCL-XL. AR42 did not alter basal chaperone activity but increased the ability of pazopanib to inhibit HSP90, HSP70 and GRP78...
January 27, 2017: Oncotarget
https://www.readbyqxmd.com/read/28128357/multilevel-interaction-of-the-dnak-dnaj-hsp70-hsp40-stress-responsive-chaperone-machine-with-the-central-metabolism
#7
Fréderic Anglès, Marie-Pierre Castanié-Cornet, Nawel Slama, Mickael Dinclaux, Anne-Marie Cirinesi, Jean-Charles Portais, Fabien Létisse, Pierre Genevaux
Networks of molecular chaperones maintain cellular protein homeostasis by acting at nearly every step in the biogenesis of proteins and protein complexes. Herein, we demonstrate that the major chaperone DnaK/HSP70 of the model bacterium Escherichia coli is critical for the proper functioning of the central metabolism and for the cellular response to carbon nutrition changes, either directly or indirectly via the control of the heat-shock response. We identified carbon sources whose utilization was positively or negatively affected by DnaK and isolated several central metabolism genes (among other genes identified in this work) that compensate for the lack of DnaK and/or DnaK/Trigger Factor chaperone functions in vivo...
January 27, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28120291/role-of-shsps-in-organizing-cytosolic-protein-aggregation-and-disaggregation
#8
REVIEW
Axel Mogk, Bernd Bukau
Small heat shock proteins (sHsps) exhibit an ATP-independent chaperone activity to prevent the aggregation of misfolded proteins in vitro. The seemingly conflicting presence of sHsps in insoluble protein aggregates in cells obstructs a precise definition of sHsp function in proteostasis networks. Recent findings specify sHsp activities in protein quality control systems. The sHsps of yeast, Hsp42 and Hsp26, interact with early unfolding intermediates of substrates, keeping them in a ready-to-refold conformation close to the native state...
January 24, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28116619/hdac6-regulates-sensitivity-to-cell-death-in-response-to-stress-and-post-stress-recovery
#9
Hyun-Wook Ryu, Hye-Rim Won, Dong Hoon Lee, So Hee Kwon
Histone deacetylase 6 (HDAC6) plays an important role in stress responses such as misfolded protein-induced aggresomes, autophagy, and stress granules. However, precisely how HDAC6 manages response during and after cellular stress remains largely unknown. This study aimed to investigate the effect of HDAC6 on various stress and post-stress recovery responses. We showed that HIF-1α protein levels were reduced in HDAC6 knockout (KO) MEFs compared to wild-type (WT) MEFs in hypoxia. Furthermore, under hypoxia, HIF-1α levels were also reduced following rescue with either a catalytically inactive or a ubiqiutin-binding mutant HDAC6...
January 23, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28104499/methylene-blue-increases-the-amount-of-hsf1-through-promotion-of-pka-mediated-increase-in-hsf1-p300-interaction
#10
Chao Huang, Wenfeng Hu, Jili Wang, Lijuan Tong, Xu Lu, Feng Wu, Yong Ling, Bo Jiang, Wei Zhang, Zhuo Chen, Qiuju Xiong, Yibin Qin, Rongrong Yang
Heat shock factor 1 (HSF1) critically contributes to the host defense, and its amount determines the mobilization efficiency of HSF1 under stress conditions. To date, how HSF1 amount is regulated remains largely unknown. We found that methylene blue (MB), an anti-oxidative and anti-inflammatory agent, increased the amount of HSF1 in BV-2 microglia, primary microglia, astrocytes, neurons and vital organs. The increased HSF1 contributed to a more increase in nuclear translocation of HSF1, association of HSF1 with heat shock protein 70 (Hsp70) promoters and Hsp70 expression levels, and also induced a synergistic protection against oxidative stress-induced injuries in MB and heat shock-treated cells...
January 16, 2017: International Journal of Biochemistry & Cell Biology
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
#11
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
#12
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
#13
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
#14
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
#15
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
#16
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
#17
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
#18
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
#19
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-heat-shock-protein-70-reveals-that-glutamic-acid-446-and-arginine-447-are-critical-for-regulating-superoxide-dismutase-2-function
#20
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...
February 10, 2017: Journal of Biological Chemistry
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