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hsp70 interacting protein

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https://www.readbyqxmd.com/read/27917864/multivalent-contacts-of-the-hsp70-ssb-contribute-to-its-architecture-on-ribosomes-and-nascent-chain-interaction
#1
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
#2
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
#3
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
https://www.readbyqxmd.com/read/27890044/effect-of-dietary-manganese-on-antioxidant-status-and-expressions-of-heat-shock-proteins-and-factors-in-tissues-of-laying-broiler-breeders-under-normal-and-high-environmental-temperatures
#4
Yong-Wen Zhu, Lin Lu, Wen-Xiang Li, Li-Yang Zhang, Cheng Ji, Xi Lin, Hsiao-Ching Liu, Jack Odle, Xu-Gang Luo
To investigate the effect of Mn on antioxidant status and on the expressions of heat shock proteins/factors in tissues of laying broiler breeders subjected to heat challenge, we used a completely randomised design (n 6) with a factorial arrangement of 2 environmental temperatures (normal, 21±1°C, and high, 32±1°C)×3 dietary Mn treatments (a Mn-unsupplemented basal diet (CON), or a basal diet supplemented with 120 mg Mn/kg diet, either as inorganic Mn sulphate (iMn) or as organic Mn proteinate (oMn)). There were no interactions (P>0·10) between environmental temperature and dietary Mn in any of the measured indices...
November 28, 2016: British Journal of Nutrition
https://www.readbyqxmd.com/read/27884606/bag3-is-a-modular-scaffolding-protein-that-physically-links-heat-shock-protein-70-hsp70-to-the-small-heat-shock-proteins
#5
Jennifer N Rauch, Eric Tse, Rebecca Freilich, Sue-Ann Mok, Leah N Makley, Daniel R Southworth, Jason E Gestwicki
Small heat shock proteins (sHsps) are a family of ATP-independent molecular chaperones that are important for binding and stabilizing unfolded proteins. In this task, the sHsps have been proposed to coordinate with ATP-dependent chaperones, including heat shock protein 70 (Hsp70). However, it is not yet clear how these two important components of the chaperone network are linked. We report that the Hsp70 co-chaperone, BAG3, is a modular, scaffolding factor to bring together sHsps and Hsp70s. Using domain deletions and point mutations, we found that BAG3 uses both of its IPV motifs to interact with sHsps, including Hsp27 (HspB1), αB-crystallin (HspB5), Hsp22 (HspB8), and Hsp20 (HspB6)...
November 21, 2016: Journal of Molecular Biology
https://www.readbyqxmd.com/read/27882919/interaction-of-the-cotranslational-hsp70-ssb-with-ribosomal-proteins-and-rrna-depends-on-its-lid-domain
#6
Andrea Gumiero, Charlotte Conz, Genís Valentín Gesé, Ying Zhang, Felix Alexander Weyer, Karine Lapouge, Julia Kappes, Ulrike von Plehwe, Géza Schermann, Edith Fitzke, Tina Wölfle, Tamás Fischer, Sabine Rospert, Irmgard Sinning
Cotranslational chaperones assist in de novo folding of nascent polypeptides in all organisms. In yeast, the heterodimeric ribosome-associated complex (RAC) forms a unique chaperone triad with the Hsp70 homologue Ssb. We report the X-ray structure of full length Ssb in the ATP-bound open conformation at 2.6 Å resolution and identify a positively charged region in the α-helical lid domain (SBDα), which is present in all members of the Ssb-subfamily of Hsp70s. Mutational analysis demonstrates that this region is strictly required for ribosome binding...
November 24, 2016: Nature Communications
https://www.readbyqxmd.com/read/27872278/reconstitution-of-a-mycobacterium-tuberculosis-proteostasis-network-highlights-essential-cofactor-interactions-with-chaperone-dnak
#7
Tania J Lupoli, Allison Fay, Carolina Adura, Michael S Glickman, Carl F Nathan
During host infection, Mycobacterium tuberculosis (Mtb) encounters several types of stress that impair protein integrity, including reactive oxygen and nitrogen species and chemotherapy. The resulting protein aggregates can be resolved or degraded by molecular machinery conserved from bacteria to eukaryotes. Eukaryotic Hsp104/Hsp70 and their bacterial homologs ClpB/DnaK are ATP-powered chaperones that restore toxic protein aggregates to a native folded state. DnaK is essential in Mycobacterium smegmatis, and ClpB is involved in asymmetrically distributing damaged proteins during cell division as a mechanism of survival in Mtb, commending both proteins as potential drug targets...
December 6, 2016: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/27868339/fasl-and-the-nkg2d-receptor-are-required-for-the-secretion-of-the-tag7-pgrp-s-hsp70-complex-by-the-cytotoxic-cd8-lymphocytes
#8
Lidia P Sashchenko, Elena A Romanova, Olga K Ivanova, Tatiana N Sharapova, Denis V Yashin
Tag7 (PGRP-S or PGLYRP1), while possessing an antimicrobial activity, also exhibits an antitumor effect when in complex with the major heat shock protein Hsp70. The cytotoxic Tag7-Hsp70 complex is secreted by lymphocytes after interaction with the HLA-negative tumors. Previously, we have shown that IL-2 induces formation of the CD4(+) and CD8(+) cytotoxic subpopulations of human lymphocytes, which kill tumor cells through the FasL-Fas interaction. Here, we show that only the CD8(+) T cells are able to secrete the Tag7-Hsp70 complex...
November 20, 2016: IUBMB Life
https://www.readbyqxmd.com/read/27863257/unraveling-the-chip-hsp70-complex-as-an-information-processor-for-protein-quality-control
#9
REVIEW
Jamie VanPelt, Richard C Page
The CHIP:Hsp70 complex stands at the crossroads of the cellular protein quality control system. Hsp70 facilitates active refolding of misfolded client proteins, while CHIP directs ubiquitination of misfolded client proteins bound to Hsp70. The direct competition between CHIP and Hsp70 for the fate of misfolded proteins leads to the question: how does the CHIP:Hsp70 complex execute triage decisions that direct misfolded proteins for either refolding or degradation? The current body of literature points toward action of the CHIP:Hsp70 complex as an information processor that takes inputs in the form of client folding state, dynamics, and posttranslational modifications, then outputs either refolded or ubiquitinated client proteins...
November 15, 2016: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/27858225/putative-model-for-heat-shock-protein-70-complexation-with-receptor-of-advanced-glycation-end-products-through-fluorescence-proximity-assays-and-normal-mode-analyses
#10
Marcelo Sartori Grunwald, Rodrigo Ligabue-Braun, Cristiane Santos Souza, Luana Heimfarth, Hugo Verli, Daniel Pens Gelain, José Cláudio Fonseca Moreira
Extracellular heat shock protein 70 (HSP70) is recognized by receptors on the plasma membrane, such as Toll-like receptor 4 (TLR4), TLR2, CD14, and CD40. This leads to activation of nuclear factor-kappa B (NF-κB), release of pro-inflammatory cytokines, enhancement of the phagocytic activity of innate immune cells, and stimulation of antigen-specific responses. However, the specific characteristics of HSP70 binding are still unknown, and all HSP70 receptors have not yet been described. Putative models for HSP70 complexation to the receptor for advanced glycation endproducts (RAGEs), considering both ADP- and ATP-bound states of HSP70, were obtained through molecular docking and interaction energy calculations...
November 17, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/27852853/coat-protein-regulation-by-ck2-cpip-hsp70-and-chip-is-required-for-potato-virus-a-replication-and-coat-protein-accumulation
#11
Andres Lõhmus, Anders Hafrén, Kristiina Mäkinen
: We demonstrate here that coat protein (CP) phosphorylation by protein kinase CK2 and a chaperone system formed by two heat-shock proteins, CP-interacting protein (CPIP) and HSP70, are both essential for Potato virus A (PVA; genus Potyvirus) replication and that all of these host proteins have the capacity to contribute to the level of PVA CP accumulation. An E3 ubiquitin ligase called carboxyl terminus Hsc70-interacting protein (CHIP), which may participate in the CPIP-HSP70-mediated CP degradation, is also needed for robust PVA gene expression...
November 16, 2016: Journal of Virology
https://www.readbyqxmd.com/read/27809308/doxorubicin-attenuates-chip-guarded-hsf1-nuclear-translocation-and-protein-stability-to-trigger-igf-iir-dependent-cardiomyocyte-death
#12
Chih-Yang Huang, Wei-Wen Kuo, Jeng-Fan Lo, Tsung-Jung Ho, Pei-Ying Pai, Shu-Fen Chiang, Pei-Yu Chen, Fu-Jen Tsai, Chang-Hai Tsai, Chih-Yang Huang
Doxorubicin (DOX) is one of the most effective antitumor drugs, but its cardiotoxicity has been a major concern for its use in cancer therapy for decades. Although DOX-induced cardiotoxicity has been investigated, the underlying mechanisms responsible for this cardiotoxicity have not been completely elucidated. Here, we found that the insulin-like growth factor receptor II (IGF-IIR) apoptotic signaling pathway was responsible for DOX-induced cardiotoxicity via proteasome-mediated heat shock transcription factor 1 (HSF1) degradation...
November 3, 2016: Cell Death & Disease
https://www.readbyqxmd.com/read/27791471/rnas-as-chaperones
#13
Scott Horowitz, James C A Bardwell
Recently, we found that RNA is a remarkably powerful chaperone that can bind to unfolded proteins and transfer them to Hsp70 for refolding. Combined with past studies on RNA-chaperone interactions, we propose a model for how chaperone RNA activity may contribute to the cellular response to stress.
October 28, 2016: RNA Biology
https://www.readbyqxmd.com/read/27787517/parp1-regulates-the-protein-stability-and-proapoptotic-function-of-hipk2
#14
Jong-Ryoul Choi, Ki Soon Shin, Cheol Yong Choi, Shin Jung Kang
Homeodomain-interacting protein kinase 2 (HIPK2) is a nuclear serine/threonine kinase that functions in DNA damage response and development. In the present study, we propose that the protein stability and proapoptotic function of HIPK2 are regulated by poly(ADP-ribose) polymerase 1 (PARP1). We present evidence indicating that PARP1 promotes the proteasomal degradation of HIPK2. The tryptophan-glycine-arginine (WGR) domain of PARP1 was necessary and sufficient for the promotion of HIPK2 degradation independently of the PARP1 enzymatic activity...
October 27, 2016: Cell Death & Disease
https://www.readbyqxmd.com/read/27783598/alternative-modes-of-client-binding-enable-functional-plasticity-of-hsp70
#15
Alireza Mashaghi, Sergey Bezrukavnikov, David P Minde, Anne S Wentink, Roman Kityk, Beate Zachmann-Brand, Matthias P Mayer, Günter Kramer, Bernd Bukau, Sander J Tans
The Hsp70 system is a central hub of chaperone activity in all domains of life. Hsp70 performs a plethora of tasks, including folding assistance, protection against aggregation, protein trafficking, and enzyme activity regulation, and interacts with non-folded chains, as well as near-native, misfolded, and aggregated proteins. Hsp70 is thought to achieve its many physiological roles by binding peptide segments that extend from these different protein conformers within a groove that can be covered by an ATP-driven helical lid...
October 26, 2016: Nature
https://www.readbyqxmd.com/read/27783273/hsp70-in-human-polymorphonuclear-and-mononuclear-leukocytes-comparison-of-the-protein-content-and-transcriptional-activity-of-hspa-genes
#16
Anna A Boyko, Tatyana L Azhikina, Maria A Streltsova, Alexander M Sapozhnikov, Elena I Kovalenko
Cell-type specific variations are typical for the expression of different members of the HSP70 family. In circulating immune cells, HSP70 proteins interact with units of signaling pathways involved in the immune responses and may promote cell survival in sites of inflammation. In this work, we compared basal HSP70 expression and stress-induced HSP70 response in polymorphonuclear and mononuclear human leukocytes. The intracellular content of inducible and constitutive forms of HSP70 was analyzed in relation to the transcriptional activity of HSPA genes...
October 25, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/27777286/interference-with-the-hsf1-hsp70-bag3-pathway-primes-glioma-cells-to-matrix-detachment-and-bh3-mimetic-induced-apoptosis
#17
Patrick Antonietti, Benedikt Linder, Stephanie Hehlgans, Iris C Mildenberger, Michael C Burger, Simone Fulda, Joachim P Steinbach, Florian Gessler, Franz Rodel, Michel Mittelbronn, Donat Kogel
Malignant gliomas exhibit a high intrinsic resistance against stimuli triggering apoptotic cell death. HSF1 (heat shock factor 1) acts as transcription factor upstream of HSP70 and the HSP70 co-chaperone BAG3 that is overexpressed in glioblastoma. To specifically target this resistance mechanism, we applied the selective HSF1 inhibitor KRIBB11 and the HSP70/BAG3 interaction inhibitor YM-1 in combination with the pan-Bcl-2 inhibitor AT-101. Here we demonstrate that lentiviral BAG3 silencing significantly enhances AT-101-induced cell death and reactivates effector caspase-mediated apoptosis in U251 glioma cells with high BAG3 expression, while these sensitizing effects were less pronounced in U343 cells expressing lower BAG3 levels...
October 24, 2016: Molecular Cancer Therapeutics
https://www.readbyqxmd.com/read/27752365/protein-arginylation-regulates-cellular-stress-response-by-stabilizing-hsp70-and-hsp40-transcripts
#18
Kamalakshi Deka, Archana Singh, Surajit Chakraborty, Rupak Mukhopadhyay, Sougata Saha
ATE1-mediated post-translational addition of arginine to a protein has been shown to regulate activity, interaction, and stability of the protein substrates. Arginylation has been linked to many different stress conditions, namely ER stress, cytosolic misfolded protein stress, and nitrosative stress. However, clear understanding about the effect of arginylation in cellular stress responses is yet to emerge. In this study, we investigated the role of arginylation in heat-stress response. Our findings suggest that Ate1 knock out (KO) cells are more susceptible to heat stress compared with its wild-type counterparts due to the induction of apoptosis in KO cells...
2016: Cell Death Discovery
https://www.readbyqxmd.com/read/27751915/defining-the-na-h-exchanger-nhe1-interactome-in-triple-negative-breast-cancer-cells
#19
Schammim Ray Amith, Krista Marie Vincent, Jodi Marie Wilkinson, Lynne Marie Postovit, Larry Fliegel
Mounting evidence supports a major role for the Na(+)/H(+) exchanger NHE1 in cancer progression and metastasis. NHE1 is hyperactive at the onset of oncogenic transformation, resulting in intracellular alkalinization and extracellular microenvironmental acidification. These conditions promote invasion and facilitate metastasis. However, the signal pathways governing the regulation of exchanger activity are still unclear. This is especially important in the aggressively metastatic, triple-negative basal breast cancer subtype...
October 15, 2016: Cellular Signalling
https://www.readbyqxmd.com/read/27744339/chaperone-families-and-interactions-in-metazoa
#20
Yael Bar-Lavan, Netta Shemesh, Anat Ben-Zvi
Quality control is an essential aspect of cellular function, with protein folding quality control being carried out by molecular chaperones, a diverse group of highly conserved proteins that specifically identify misfolded conformations. Molecular chaperones are thus required to support proteins affected by expressed polymorphisms, mutations, intrinsic errors in gene expression, chronic insult or the acute effects of the environment, all of which contribute to a flux of metastable proteins. In this article, we review the four main chaperone families in metazoans, namely Hsp60 (where Hsp is heat-shock protein), Hsp70, Hsp90 and sHsps (small heat-shock proteins), as well as their co-chaperones...
October 15, 2016: Essays in Biochemistry
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