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hsp70 interacting protein

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https://www.readbyqxmd.com/read/28322872/plasmodium-hsp40-and-human-hsp70-a-potential-cochaperone-chaperone-complex
#1
Payal Jha, Shyamasree Laskar, Swati Dubey, Mrinal K Bhattacharyya, Sunanda Bhattacharyya
Out of the total forty four members of Plasmodium falciparum Hsp40 protein family, nineteen of them possess a PEXEL motif, and are predicted to be exported into the cytosol of an infected RBC. It is speculated that the human Hsp70 (hHsp70), which resides into the cytosol of the host erythrocyte, along with the exported PfHsp40s assists in the folding of parasitic proteins, thus playing a crucial role in the establishment of virulence. However, till date no experimental evidence supports this hypothesis. Our work establishes that the PEXEL motifs containing Type II PfDNAJ proteins specifically interact with hHsp70 (HSPA1A)...
March 16, 2017: Molecular and Biochemical Parasitology
https://www.readbyqxmd.com/read/28322792/molecular-chaperones-of-the-hsp70-family-assist-in-the-assembly-of-20s-proteasomes
#2
Lindsay J Hammack, Kyle Firestone, William Chang, Andrew R Kusmierczyk
The eukaryotic 26S proteasome is a large protease comprised of two major sub assemblies, the 20S proteasome, or core particle (CP), and the 19S regulatory particle (RP). Assembly of the CP and RP is assisted by an expanding list of dedicated assembly factors. For the CP, this includes Ump1 and the heterodimeric Pba1-Pba2 and Pba3-Pba4 proteins. It is not known how many additional proteins that assist in proteasome biogenesis remain to be discovered. Here, we demonstrate that two members of the Hsp70 family in yeast, Ssa1 and Ssa2, play a direct role in CP assembly...
March 17, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28320739/a-covalently-bound-inhibitor-triggers-ezh2-degradation-through-chip-mediated-ubiquitination
#3
Xu Wang, Wei Cao, Jianjun Zhang, Ming Yan, Qin Xu, Xiangbing Wu, Lixin Wan, Zhiyuan Zhang, Chenping Zhang, Xing Qin, Meng Xiao, Dongxia Ye, Yuyang Liu, Zeguang Han, Shaomeng Wang, Li Mao, Wenyi Wei, Wantao Chen
Enhancer of zeste homolog 2 (EZH2) has been characterized as a critical oncogene and a promising drug target in human malignant tumors. The current EZH2 inhibitors strongly suppress the enhanced enzymatic function of mutant EZH2 in some lymphomas. However, the recent identification of a PRC2- and methyltransferase-independent role of EZH2 indicates that a complete suppression of all oncogenic functions of EZH2 is needed. Here, we report a unique EZH2-targeting strategy by identifying a gambogenic acid (GNA) derivative as a novel agent that specifically and covalently bound to Cys668 within the EZH2-SET domain, triggering EZH2 degradation through COOH terminus of Hsp70-interacting protein (CHIP)-mediated ubiquitination...
March 20, 2017: EMBO Journal
https://www.readbyqxmd.com/read/28314505/how-do-j-proteins-get-hsp70-to-do-so-many-different-things
#4
REVIEW
Elizabeth A Craig, Jaroslaw Marszalek
Hsp70 chaperone machineries have pivotal roles in an array of fundamental biological processes through their facilitation of protein folding, disaggregation, and remodeling. The obligate J-protein co-chaperones of Hsp70s drive much of this remarkable multifunctionality, with most Hsp70s having multiple J-protein partners. Recent data suggest that J-protein-driven versatility is substantially due to precise localization within the cell and the specificity of substrate protein binding. However, this relatively simple view belies the intricacy of J-protein function...
March 14, 2017: Trends in Biochemical Sciences
https://www.readbyqxmd.com/read/28294381/cd3-cd8-nkg2d-t-lymphocytes-induce-apoptosis-and-necroptosis-in-hla-negative-cells-via-fasl-fas-interaction
#5
O K Ivanova, T N Sharapova, E A Romanova, L P Sashchenko, D V Yashin
An important problem in cellular immunology is to identify new populations of cytotoxic lymphocytes capable of killing tumor cells that have lost classical components of MHC-machinery and to understand mechanisms of the death of these cells. We have previously found that CD4(+) CD25(+) lymphocytes appear in the lymphokine-activated killer (LAK) cell culture, which carry Tag7 (PGRP-S) and FasL proteins on their surface and can kill Hsp70- and Fas-expressing HLA-negative cells. In this work, we have continued to study the mechanisms of killing of the HLA-negative tumor cells, focusing this time on the CD8+ lymphocytes...
March 15, 2017: Journal of Cellular Biochemistry
https://www.readbyqxmd.com/read/28293543/the-tudor-staphylococcal-nuclease-protein-of-entamoeba-histolytica-participates-in-transcription-regulation-and-stress-response
#6
Javier Cázares-Apátiga, Christian Medina-Gómez, Bibiana Chávez-Munguía, Mercedes Calixto-Gálvez, Esther Orozco, Carlos Vázquez-Calzada, Aarón Martínez-Higuera, Mario A Rodríguez
Entamoeba histolytica is the protozoa parasite responsible of human amoebiasis, disease that causes from 40,000 to 100,000 deaths annually worldwide. However, few are known about the expression regulation of molecules involved in its pathogenicity. Transcription of some virulence-related genes is positively controlled by the cis-regulatory element named URE1. Previously we identified the transcription factor that binds to URE1, which displayed a nuclear and cytoplasmic localization. This protein belongs to the Tudor Staphyococcal nuclease (TSN) family, which in other systems participates in virtually all pathways of gene expression, suggesting that this amoebic transcription factor (EhTSN; former EhURE1BP) could also play multiple functions in E...
2017: Frontiers in Cellular and Infection Microbiology
https://www.readbyqxmd.com/read/28286332/two-alternative-binding-mechanisms-connect-the-protein-translocation-sec71-sec72-complex-with-heat-shock-proteins
#7
Arati Tripathi, Elisabet C Mandon, Reid Gilmore, Tom A Rapoport
The biosynthesis of many eukaryotic proteins requires accurate targeting to and translocation across the endoplasmic reticulum (ER) membrane. Post-translational protein translocation in yeast requires both the Sec61 translocation channel, and a complex of four additional proteins: Sec63, Sec62, Sec71, and Sec72. The structure and function of these proteins are largely unknown. This pathway also requires the cytosolic Hsp70 protein Ssa1, but whether Ssa1 associates with the translocation machinery to target protein substrates to the membrane is unclear...
March 12, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28286098/hepatic-gene-expression-profiles-of-a-non-model-cyprinid-barbus-plebejus-chronically-exposed-to-river-sediments
#8
Nadia Casatta, Fabrizio Stefani, Luigi Viganò
In this study, we characterized the gene expression responses of the Padanian barbel (Barbus plebejus), a native benthivorous cyprinid with a very compromised presence within the fish community of the River Po. Barbel juveniles were exposed in the laboratory to two river sediments reflecting an upstream/downstream gradient of increasing contamination and collected from one of the most anthropized tributaries of the River Po. After 7months of exposure, hepatic transcriptional changes that were diagnostic of sediment exposure were assessed...
March 9, 2017: Comparative Biochemistry and Physiology. Toxicology & Pharmacology: CBP
https://www.readbyqxmd.com/read/28278223/the-structure-of-fkbp38-in-complex-with-the-meevd-tetratricopeptide-binding-motif-of-hsp90
#9
Katie L I M Blundell, Mohinder Pal, S Mark Roe, Laurence H Pearl, Chrisostomos Prodromou
Tetratricopeptide (TPR) domains are known protein interaction domains. We show that the TPR domain of FKBP8 selectively binds Hsp90, and interactions upstream of the conserved MEEVD motif are critical for tight binding. In contrast FKBP8 failed to bind intact Hsp70. The PPIase domain was not essential for the interaction with Hsp90 and binding was completely encompassed by the TPR domain alone. The conformation adopted by Hsp90 peptides, containing the conserved MEEVD motif, in the crystal structure were similar to that seen for the TPR domains of CHIP, AIP and Tah1...
2017: PloS One
https://www.readbyqxmd.com/read/28261750/partial-dispensability-of-djp1-s-j-domain-in-peroxisomal-protein-import-in-saccharomyces-cerevisiae-results-from-genetic-redundancy-with-another-class-ii-j-protein-caj1
#10
Neha Dobriyal, Prerna Tripathi, Susrita Sarkar, Yogesh Tak, Amit K Verma, Chandan Sahi
J proteins are obligate co-chaperones of Hsp70s. Via their signature J domain, all J proteins interact with their partner Hsp70s and stimulate their weak ATPase activity, which is vital for Hsp70 functions. The dependency of J proteins on their J domain is such that mutations in critical amino acids in the J domain often results into a null phenotype for a particular J protein. Here, we show that the J domain of Djp1, a cytosolic J protein important for peroxisomal protein import in Saccharomyces cerevisiae, is partially dispensable...
March 6, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28243524/intersexual-differences-of-heat-shock-response-between-two-amphipods-eulimnogammarus-verrucosus-and-eulimnogammarus-cyaneus-in-lake-baikal
#11
Daria Bedulina, Michael F Meyer, Anton Gurkov, Ekaterina Kondratjeva, Boris Baduev, Roman Gusdorf, Maxim A Timofeyev
Acute temperature fluctuations are common in surface waters, and aquatic organisms may manifest physiological responses to punctuated temperature spikes long before behavioral responses. Ectotherms, especially cryophilic stenotherms such as those endemic to Lake Baikal (Siberia), may demonstrate specialized physiological responses to acute temperature increases because their proteomes have evolved to function most efficiently at lower temperatures (e.g., <10 °C). Therefore, our study questioned the nature and degree of variation in physiological response to acute thermal stress in two congenerous, endemic Baikal amphipod species, Eulimnogammarus verrucosus and Eulimnogammarus cyaneus...
2017: PeerJ
https://www.readbyqxmd.com/read/28224252/heat-shock-protein-70-in-lung-and-kidney-of-specific-pathogen-free-chickens-is-a-receptor-associated-protein-that-interacts-with-the-binding-domain-of-the-spike-protein-of-infectious-bronchitis-virus
#12
ZhiKun Zhang, Xin Yang, PengWei Xu, Xuan Wu, Long Zhou, HongNing Wang
Avian infectious bronchitis virus (IBV) is a member of the family Coronaviridae. A binding domain that mediates the attachment of the virus to its receptor has been identified in the S1 protein of prototype IBV strain M41. In this study, we identified this binding domain in a different strain, as well as the cellular proteins that interact with it. First, we expressed the S1N proteins (residues 19-270) of M41 and another isolate, SCZJ3, and compared the binding capacities of recombinant S1N-M41 and S1N-SCZJ3 to host tissues...
February 21, 2017: Archives of Virology
https://www.readbyqxmd.com/read/28224177/joint-toxicity-of-arsenic-copper-and-glyphosate-on-behavior-reproduction-and-heat-shock-protein-response-in-caenorhabditis-elegans
#13
Yunbiao Wang, Anastasia N Ezemaduka, Zhuheng Li, Zhanyan Chen, Chuantao Song
The soil nematode Caenorhabditis elegans was used in 24-h acute exposures to arsenic (As), copper (Cu) and glyphosate (GPS) and to mixtures of As/Cu and As/GPS to investigate the effects of mixture exposures in the worms. A synergistic type of interaction was observed for acute toxicity with the As/Cu and As/GPS mixtures. Sublethal 24-h exposures of 1/1000, 1/100 and 1/10 of the LC50 concentrations for As, Cu and GPS individually and for As/Cu and As/GPS mixtures were conducted to observe responses in locomotory behavior (head thrashing), reproduction, and heat shock protein expression...
April 2017: Bulletin of Environmental Contamination and Toxicology
https://www.readbyqxmd.com/read/28220454/the-remarkable-multivalency-of-the-hsp70-chaperones
#14
REVIEW
Erik R P Zuiderweg, Lawrence E Hightower, Jason E Gestwicki
Hsp70 proteins are key to maintaining intracellular protein homeostasis. To carry out this task, they employ a large number of cochaperones and adapter proteins. Here, we review what is known about the interaction between the chaperones and partners, with a strong slant toward structural biology. Hsp70s in general, and Hsc70 (HSPA8) in particular, display an amazing array of interfaces with their protein cofactors. We also review the known interactions between Hsp70s with lipids and with active compounds that may become leads toward Hsp70 modulation for treatment of a variety of diseases...
February 20, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28218284/proteomic-analysis-of-exported-chaperone-co-chaperone-complexes-of-p-falciparum-reveals-an-array-of-complex-protein-protein-interactions
#15
Qi Zhang, Cheng Ma, Alexander Oberli, Astrid Zinz, Sonja Engels, Jude M Przyborski
Malaria parasites modify their human host cell, the mature erythrocyte. This modification is mediated by a large number of parasite proteins that are exported to the host cell, and is also the underlying cause for the pathology caused by malaria infection. Amongst these proteins are many Hsp40 co-chaperones, and a single Hsp70. These proteins have been implicated in several processes in the host cell, including a potential role in protein transport, however the further molecular players in this process remain obscure...
February 20, 2017: Scientific Reports
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
#16
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
#17
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
#18
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
#19
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
#20
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
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