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hsp70 interacting protein

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https://www.readbyqxmd.com/read/28819167/artificial-dnaj-protein-for-protein-production-and-conformational-diseases
#1
Akinori Hishiya, Keizo Koya
For secreted proteins, proper protein folding is essential not only for biological function but also for secretion itself. Proteins with folding problems are trapped in the endoplasmic reticulum (ER) and are eventually degraded in the cytoplasm. In this study, we exploited co-expression of an artificial fusion protein, based on the sequence of a DnaJ protein, which could interact as co-chaperones in the Hsp70-based protein-folding system, with target recombinant secreted proteins to enhance their production and secretion...
August 17, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28819163/fusion-protein-analysis-reveals-the-precise-regulation-between-hsp70-and-hsp100-during-protein-disaggregation
#2
Sayaka Hayashi, Yosuke Nakazaki, Kei Kagii, Hiromi Imamura, Yo-Hei Watanabe
ClpB, a bacterial Hsp100, is a ring-shaped AAA+ chaperone that can reactivate aggregated proteins in cooperation with DnaK, a bacterial Hsp70, and its co-factors. ClpB subunits comprise two AAA+ modules with an interstitial rod-shaped M-domain. The M-domain regulates ClpB ATPase activity and interacts directly with the DnaK nucleotide-binding domain (NBD). Here, to clarify how these functions contribute to the disaggregation process, we constructed ClpB, DnaK, and aggregated YFP fusion proteins in various combinations...
August 17, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28792733/crohn-s-disease-variants-of-nod2-are-stabilized-by-critical-contact-region-of-hsp70
#3
Amy K Schaefer, Hannah Wastyk, Vishnu Mohanan, Ching-Wen Hou, Mackenzie L Lauro, James E Melnyk, Catherine Leimkuhler Grimes
Nod2 is a cytosolic, innate immune receptor responsible for binding to bacterial cell wall fragments such as muramyl dipeptide (MDP). Upon binding, subsequent downstream activation of the NF-κB pathway leads to an immune response. Nod2 mutations are correlated with an increased susceptibility for Crohn's disease (CD) and ultimately results in a misregulated immune response. Previous work had demonstrated that Nod2 interacts with and is stabilized by the molecular chaperone Hsp70. In this work it is shown using purified protein and in vitro bio-chemical assays that the critical Nod2 CD mutations (G908R, R702W, 1007fs) retain the ability to bind bacterial ligands...
August 9, 2017: Biochemistry
https://www.readbyqxmd.com/read/28771464/two-chaperones-locked-in-an-embrace-structure-and-function-of-the-ribosome-associated-complex-rac
#4
REVIEW
Ying Zhang, Irmgard Sinning, Sabine Rospert
Chaperones, which assist protein folding are essential components of every living cell. The yeast ribosome-associated complex (RAC) is a chaperone that is highly conserved in eukaryotic cells. The RAC consists of the J protein Zuo1 and the unconventional Hsp70 homolog Ssz1. The RAC heterodimer stimulates the ATPase activity of the ribosome-bound Hsp70 homolog Ssb, which interacts with nascent polypeptide chains to facilitate de novo protein folding. In addition, the RAC-Ssb system is required to maintain the fidelity of protein translation...
August 3, 2017: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/28770685/insulin-igf-signaling-and-life-history-traits-in-response-to-food-availability-and-perceived-density-in-the-cnidarian-hydra-vulgaris
#5
Flóra Sebestyén, Szilárd Póliska, Rita Rácz, Judit Bereczki, Kinga Lénárt, Zoltán Barta, Ádám Z Lendvai, Jácint Tökölyi
Insulin/insulin-like growth factor signaling (IIS) is thought to be a central mediator of life history traits, but the generality of its role is not clear. Here, we investigated mRNA expression levels of three insulin-like peptide genes, the insulin-like receptor htk7, as well as several antioxidant genes, and the heat-shock protein hsp70 in the freshwater cnidarian Hydra vulgaris. Hydra polyps were exposed to a combination of different levels of food and perceived population density to manipulate life history traits (asexual reproduction and oxidative stress tolerance)...
August 2017: Zoological Science
https://www.readbyqxmd.com/read/28769758/the-role-of-bip-retrieval-by-the-kdel-receptor-in-the-early-secretory-pathway-and-its-effect-on-protein-quality-control-and-neurodegeneration
#6
REVIEW
Hisayo Jin, Mari Komita, Tomohiko Aoe
Protein quality control in the early secretory pathway is a ubiquitous eukaryotic mechanism for adaptation to endoplasmic reticulum (ER) stress. An ER molecular chaperone, immunoglobulin heavy chain-binding protein (BiP), is one of the essential components in this process. BiP interacts with nascent proteins to facilitate their folding. BiP also plays an important role in preventing aggregation of misfolded proteins and regulating the ER stress response when cells suffer various injuries. BiP is a member of the 70-kDa heat shock protein (HSP70) family of molecular chaperones that resides in the ER...
2017: Frontiers in Molecular Neuroscience
https://www.readbyqxmd.com/read/28757353/osmotic-and-heat-stress-dependent-regulation-of-mlk4%C3%AE-and-mlk3-by-the-chip-e3-ligase-in-ovarian-cancer-cells
#7
Natalya A Blessing, Srimathi Kasturirangan, Evan M Zink, April L Schroyer, Deborah N Chadee
Mixed Lineage Kinase 3 (MLK3), a member of the MLK subfamily of protein kinases, is a mitogen-activated protein (MAP) kinase kinase kinase (MAP3K) that activates MAPK signalling pathways and regulates cellular responses such as proliferation, invasion and apoptosis. MLK4β, another member of the MLK subfamily, is less extensively studied, and the regulation of MLK4β by stress stimuli is not known. In this study, the regulation of MLK4β and MLK3 by osmotic stress, thermostress and heat shock protein 90 (Hsp90) inhibition was investigated in ovarian cancer cells...
July 28, 2017: Cellular Signalling
https://www.readbyqxmd.com/read/28754691/the-hsp70-interdomain-linker-is-a-dynamic-switch-that-enables-allosteric-communication-between-two-structured-domains
#8
Charles A English, Woody Sherman, Wenli Meng, Lila M Gierasch
Hsp70 molecular chaperones play key roles in cellular protein homeostasis by binding to exposed hydrophobic regions of incompletely folded or aggregated proteins. This crucial Hsp70 function relies on allosteric communication between two well-structured domains: an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD), which are tethered by an interdomain linker. ATP or ADP binding to the NBD alters the substrate-binding affinity of the SBD, triggering functionally essential cycles of substrate binding and release...
July 28, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28745541/chaperone-proteins-as-single-component-reagents-to-assess-antibody-nonspecificity
#9
Ryan L Kelly, James C Geoghegan, Jared Feldman, Tushar Jain, Monique Kauke, Doris Le, Jessie Zhao, K Dane Wittrup
Early stage assays that evaluate monoclonal antibody drug-like properties serve as valuable tools for selection of lead candidates. One liability for clinical development, off-target reactivity, is often assessed by binding to a mixture or panel of noncognate proteins. While robust, these mixes are often ill-defined, and can suffer from issues such as lot-to-lot variability. In this study, we discovered in immunoprecipitation experiments that certain chaperones are present in one of these mixtures; we then explored the use of recombinant chaperone proteins as well-characterized agents to predict antibody nonspecificity...
July 26, 2017: MAbs
https://www.readbyqxmd.com/read/28737514/bag3-plays-a-central-role-in-proteostasis-in-the-heart
#10
Wataru Mizushima, Junichi Sadoshima
Proteinopathies are characterized by the accumulation of misfolded proteins, which ultimately interfere with normal cell function. While neurological diseases, such as Huntington disease and Alzheimer disease, are well-characterized proteinopathies, cardiac diseases have recently been associated with alterations in proteostasis. In this issue of the JCI, Fang and colleagues demonstrate that mice with cardiac-specific deficiency of the co-chaperone protein BCL2-associated athanogene 3 (BAG3) develop dilated cardiomyopathy that is associated with a destabilization of small HSPs as the result of a disrupted interaction between BAG3 and HSP70...
August 1, 2017: Journal of Clinical Investigation
https://www.readbyqxmd.com/read/28737513/loss-of-function-mutations-in-co-chaperone-bag3-destabilize-small-hsps-and-cause-cardiomyopathy
#11
Xi Fang, Julius Bogomolovas, Tongbin Wu, Wei Zhang, Canzhao Liu, Jennifer Veevers, Matthew J Stroud, Zhiyuan Zhang, Xiaolong Ma, Yongxin Mu, Dieu-Hung Lao, Nancy D Dalton, Yusu Gu, Celine Wang, Michael Wang, Yan Liang, Stephan Lange, Kunfu Ouyang, Kirk L Peterson, Sylvia M Evans, Ju Chen
Defective protein quality control (PQC) systems are implicated in multiple diseases. Molecular chaperones and co-chaperones play a central role in functioning PQC. Constant mechanical and metabolic stress in cardiomyocytes places great demand on the PQC system. Mutation and downregulation of the co-chaperone protein BCL-2-associated athanogene 3 (BAG3) are associated with cardiac myopathy and heart failure, and a BAG3 E455K mutation leads to dilated cardiomyopathy (DCM). However, the role of BAG3 in the heart and the mechanisms by which the E455K mutation leads to DCM remain obscure...
August 1, 2017: Journal of Clinical Investigation
https://www.readbyqxmd.com/read/28725639/anaplasma-phagocytophilum-msp4-and-hsp70-proteins-are-involved-in-interactions-with-host-cells-during-pathogen-infection
#12
Marinela Contreras, Pilar Alberdi, Lourdes Mateos-Hernández, Isabel G Fernández de Mera, Ana L García-Pérez, Marie Vancová, Margarita Villar, Nieves Ayllón, Alejandro Cabezas-Cruz, James J Valdés, Snorre Stuen, Christian Gortazar, José de la Fuente
Anaplasma phagocytophilum transmembrane and surface proteins play a role during infection and multiplication in host neutrophils and tick vector cells. Recently, A. phagocytophilum Major surface protein 4 (MSP4) and Heat shock protein 70 (HSP70) were shown to be localized on the bacterial membrane, with a possible role during pathogen infection in ticks. In this study, we hypothesized that A. phagocytophilum MSP4 and HSP70 have similar functions in tick-pathogen and host-pathogen interactions. To address this hypothesis, herein we characterized the role of these bacterial proteins in interaction and infection of vertebrate host cells...
2017: Frontiers in Cellular and Infection Microbiology
https://www.readbyqxmd.com/read/28711525/novel-hsp90-inhibitor-platycodin-d-disrupts-hsp90-cdc37-complex-and-enhances-the-anticancer-effect-of-mtor-inhibitor
#13
Ting Li, Xin Chen, Xiao-Yang Dai, Bin Wei, Qin-Jie Weng, Xiuping Chen, De-Fang Ouyang, Ru Yan, Zhang-Jian Huang, Hu-Lin Jiang, Hong Zhu, Jin-Jian Lu
Heat shock protein 90 (Hsp90) is a critically conserved molecular chaperone protein and promising therapeutic target for cancer treatment. In this study, platycodin D (PD), a saponin isolated from traditional Chinese herb Platycodonis Radix, was identified as a novel Hsp90 inhibitor. We verified that PD did not affect the ATPase activity of Hsp90. However, PD disrupted the co-chaperone interaction of Hsp90/cell division cycle protein 37 (Cdc37) and subsequently degraded multiple Hsp90 client proteins without the feedback increase of Hsp70...
September 1, 2017: Toxicology and Applied Pharmacology
https://www.readbyqxmd.com/read/28708998/profiling-ssb-nascent-chain-interactions-reveals-principles-of-hsp70-assisted-folding
#14
Kristina Döring, Nabeel Ahmed, Trine Riemer, Harsha Garadi Suresh, Yevhen Vainshtein, Markus Habich, Jan Riemer, Matthias P Mayer, Edward P O'Brien, Günter Kramer, Bernd Bukau
The yeast Hsp70 chaperone Ssb interacts with ribosomes and nascent polypeptides to assist protein folding. To reveal its working principle, we determined the nascent chain-binding pattern of Ssb at near-residue resolution by in vivo selective ribosome profiling. Ssb associates broadly with cytosolic, nuclear, and hitherto unknown substrate classes of mitochondrial and endoplasmic reticulum (ER) nascent proteins, supporting its general chaperone function. Ssb engages most substrates by multiple binding-release cycles to a degenerate sequence enriched in positively charged and aromatic amino acids...
July 13, 2017: Cell
https://www.readbyqxmd.com/read/28708484/promiscuous-binding-by-hsp70-results-in-conformational-heterogeneity-and-fuzzy-chaperone-substrate-ensembles
#15
Rina Rosenzweig, Ashok Sekhar, Jayashree Nagesh, Lewis E Kay
The Hsp70 chaperone system is integrated into a myriad of biochemical processes that are critical for cellular proteostasis. Although detailed pictures of Hsp70 bound with peptides have emerged, correspondingly detailed structural information on complexes with folding-competent substrates remains lacking. Here we report a methyl-TROSY based solution NMR study showing that the Escherichia coli version of Hsp70, DnaK, binds to as many as four distinct sites on a small 53-residue client protein, hTRF1. A fraction of hTRF1 chains are also bound to two DnaK molecules simultaneously, resulting in a mixture of DnaK-substrate sub-ensembles that are structurally heterogeneous...
July 14, 2017: ELife
https://www.readbyqxmd.com/read/28704482/proteomic-identification-of-proteins-differentially-expressed-following-overexpression-of-htert-human-telomerase-reverse-transcriptase-in-cancer-cells
#16
Rishi Kumar Jaiswal, Pramod Kumar, Amod Sharma, Deepak Kumar Mishra, Pramod Kumar Yadava
Reverse transcriptase activity of telomerase adds telomeric repeat sequences at extreme ends of the newly replicated chromosome in actively dividing cells. Telomerase expression is not detected in terminally differentiated cells but is noticeable in 90% of the cancer cells. hTERT (human telomerase reverse transcriptase) expression seems to promote invasiveness of cancer cells. We here present proteomic profiles of cells overexpressing or knocked down for hTERT. This study also attempts to find out the potential interacting partners of hTERT in cancer cell lines...
2017: PloS One
https://www.readbyqxmd.com/read/28696498/hsp70-a-master-regulator-in-protein-degradation
#17
REVIEW
M Rosario Fernández-Fernández, Marcos Gragera, Lissette Ochoa-Ibarrola, Lucía Quintana-Gallardo, José María Valpuesta
Proteostasis, the controlled balance of protein synthesis, folding, assembly, trafficking and degradation, is a paramount necessity for cell homeostasis. Impaired proteostasis is a hallmark of ageing and of many human diseases. Molecular chaperones are essential for proteostasis in eukaryotic cells, and their function has traditionally been linked to protein folding, assembly and disaggregation. More recent findings suggest that chaperones also contribute to key steps in protein degradation. In particular, Hsp70 has an essential role in substrate degradation through the ubiquitin-proteasome system, as well as through different autophagy pathways...
July 11, 2017: FEBS Letters
https://www.readbyqxmd.com/read/28691182/heat-shock-protein-70-inhibitors-suppress-androgen-receptor-expression-in-lncap95-prostate-cancer-cells
#18
Kazuaki Kita, Masayuki Shiota, Masako Tanaka, Asuka Otsuka, Masaki Matsumoto, Minoru Kato, Satoshi Tamada, Hiroshi Iwao, Katsuyuki Miura, Tatsuya Nakatani, Shuhei Tomita
Androgen deprivation therapy is initially effective for treating patients with advanced prostate cancer; however, the prostate cancer gradually becomes resistant to androgen deprivation therapy, which is termed castration-resistant prostate cancer (CRPC). Androgen receptor splice variant 7 (AR-V7), one of the causes of CRPC, is correlated with resistance to a new-generation AR antagonist (enzalutamide) and poor prognosis. Heat shock protein 70 (Hsp70) inhibitor is known to decrease the levels of full-length AR (AR-FL), but little is known about its effects against CRPC cells expressing AR-V7...
July 10, 2017: Cancer Science
https://www.readbyqxmd.com/read/28686685/comparative-proteomic-analysis-of-gib2-validating-its-adaptor-function-in-cryptococcus-neoformans
#19
Gillian O Bruni, Blake Battle, Ben Kelly, Zhengguang Zhang, Ping Wang
Cryptococcus neoformans causes often-fatal fungal meningoencephalitis in immunocompromised individuals. While the exact disease mechanisms remain elusive, signal transduction pathways mediated by key elements such as G-protein α subunit Gpa1, small GTPase Ras1, and atypical Gβ-like/RACK1 protein Gib2 are known to play important roles in C. neoformans virulence. Gib2 is important for normal growth, differentiation, and pathogenicity, and it also positively regulates cAMP levels in conjunction with Gpa1. Interestingly, Gib2 displays a scaffold protein property by interacting with a wide variety of cellular proteins...
2017: PloS One
https://www.readbyqxmd.com/read/28685898/the-hsp40-j-domain-modulates-hsp70-conformation-and-atpase-activity-with-a-semi-elliptical-spring
#20
Neil Andrew D Bascos, Matthias P Mayer, Bernd Bukau, Samuel J Landry
Regulatory protein interactions are commonly attributed to lock-and-key associations that bring interacting domains together. However, studies in some systems suggest that regulation is not achieved by binding interactions alone. We report our investigations on specific physical characteristics required of the Hsp40 J-domain to stimulate ATP hydrolysis in the Hsp40-Hsp70 molecular chaperone machine. Biophysical analysis using isothermal titration calorimetry, and nuclear magnetic resonance spectroscopy reveals the importance of helix rigidity for the maintenance of Hsp40 function...
July 7, 2017: Protein Science: a Publication of the Protein Society
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