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Protein chaperones

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https://www.readbyqxmd.com/read/29666470/glucose-regulated-protein-78-is-essential-for-cardiac-myocyte-survival
#1
Xiaoding Wang, Xukun Bi, Guangyu Zhang, Yingfeng Deng, Xiang Luo, Lin Xu, Philipp E Scherer, Anwarul Ferdous, Guosheng Fu, Thomas G Gillette, Amy S Lee, Xuejun Jiang, Zhao V Wang
Secretory and transmembrane proteins rely on proper function of the secretory pathway for folding, posttranslational modification, assembly, and secretion. Accumulation of misfolded proteins in the endoplasmic reticulum (ER) stimulates the unfolded protein response (UPR), which communicates between the ER and other organelles to enhance ER-folding capacity and restore cellular homeostasis. Glucose-regulated protein of 78 kDa (GRP78), an ER-resident protein chaperone, is a master regulator of all UPR signaling branches...
April 17, 2018: Cell Death and Differentiation
https://www.readbyqxmd.com/read/29666155/sil1-the-er-hsp70-co-chaperone-plays-a-critical-role-in-maintaining-skeletal-muscle-proteostasis-and-physiology
#2
Viraj P Ichhaporia, Jieun Kim, Kanisha Kavdia, Peter Vogel, Linda Horner, Sharon Frase, Linda M Hendershot
Mutations in SIL1 , a co-factor for the endoplasmic reticular (ER) chaperone BiP, cause Marinesco-Sjögren syndrome (MSS), an autosomal recessive disorder. Using a mouse model, we characterized molecular aspects of the progressive myopathy associated with MSS. Proteomic-profiling of quadriceps at the onset of myopathy revealed that SIL1 deficiency affected multiple pathways critical to muscle physiology. We observed an increase in ER chaperones prior to the onset of muscle weakness, which was complemented by up-regulation of multiple components of cellular protein degradation pathways...
April 9, 2018: Disease Models & Mechanisms
https://www.readbyqxmd.com/read/29665050/silence-of-hdac6-suppressed-esophageal-squamous-cell-carcinoma-proliferation-and-migration-by-disrupting-chaperone-function-of-hsp90
#3
Hua Tao, Yuan-Yuan Chen, Zong-Wen Sun, Hua-Lin Chen, Ming Chen
Esophageal carcinoma is aggressive in nature and its prognosis is largely dependent on the degree of invasion. Histone deacetylase 6 (HDAC6), as the most unique member of HDACs family, has the positive activity to promote initiation and progression of various cancers via targeting multiple non-histone proteins in cytoplasm. In this study, we found that HDAC6 was over-expressed in three esophageal cancer cell lines (KYSE140, KYSE170, KYSE180) when compared to non-carcinoma esophageal epithelial cell HEEC-1. Then two HDAC6 specific siRNAs and HDAC6 inhibitor tubastatin A greatly suppressed KYSE140 and KYSE180 cells proliferation and migration, and the inhibition of cell motility was accompanied by elevated acetylation of α-tubulin, a target of HDAC6...
April 17, 2018: Journal of Cellular Biochemistry
https://www.readbyqxmd.com/read/29665007/protective-effect-of-mir378-on-doxorubicin-induced-cardiomyocyte-injury-via-calumenin
#4
Yu Wang, Xiaoxue Cui, Yilin Wang, Yao Fu, Xin Guo, Jie Long, Chengxi Wei, Ming Zhao
Doxorubicin (Dox) is a highly effective antitumor antibiotic, however myocardial toxicity severely limits its use clinically. The pathogenesis of doxorubicin-induced cardiomyopathy is unclear. In Dox cardiomyopathy mice, there is a decline in cardiac function, a change in myocardial pathology and a reduction in miR378* expression. Expression changes in calumenin, an endoplasmic reticulum stress (ERS) chaperone protein and pathway factor, as well as apoptosis, were observed in cardiomyocytes after doxorubicin-induced injury...
April 17, 2018: Journal of Cellular Physiology
https://www.readbyqxmd.com/read/29663867/coiled-coil-and-leucine-rich-repeat-domain-of-the-potyvirus-resistance-protein-pvr4-has-distinct-role-in-signaling-and-pathogen-recognition
#5
Saet-Byul Kim, Hye-Young Lee, Eun-Hye Choi, Eunsook Park, Jihyun Kim, Ki-Beom Moon, Hyun-Soon Kim, Doil Choi
The pepper Pvr4 encoding coiled-coil (CC) nucleotide-binding (NB) leucine-rich repeat (LRR) protein (CC-NLR) confer hypersensitive resistance (HR) to potyviruses, including Pepper mottle virus (PepMoV) by recognizing the viral avirulence protein, NIb. To figure out the Pvr4-mediated HR mechanism, we analyzed the signaling component genes and structure-function relationships of Pvr4 using chimeras and deletion mutants in Nicotiana benthamiana. Molecular chaperone components including HSP90, SGT1 and RAR1 were required, while plant hormones and mitogen-activated protein (MAP) kinase signaling components had little effect on Pvr4-NIb-mediated HR cell death...
April 17, 2018: Molecular Plant-microbe Interactions: MPMI
https://www.readbyqxmd.com/read/29662477/new-genes-involved-in-mild-stress-response-identified-by-transposon-mutagenesis-in-lactobacillus-paracasei
#6
Aurore Palud, Hélène Scornec, Jean-François Cavin, Hélène Licandro
Lactic acid bacteria (LAB) are associated with various plant, animal, and human niches and are also present in many fermented foods and beverages. Thus, they are subjected to several stress conditions and have developed advanced response mechanisms to resist, adapt, and grow. This work aimed to identify the genes involved in some stress adaptation mechanisms in LAB. For this purpose, global reverse genetics was applied by screening a library of 1287 Lactobacillus paracasei transposon mutants for mild monofactorial stresses...
2018: Frontiers in Microbiology
https://www.readbyqxmd.com/read/29662435/ac2-26-induces-ikk%C3%AE-degradation-through-chaperone-mediated-autophagy-via-hspb1-in-ncm-treated-microglia
#7
Lu Liu, Dandan An, Junying Xu, Bin Shao, Xing Li, Jing Shi
Annexin A1 (ANXA1) is an endogenous protein with potent anti-inflammatory properties in the brain. Although ANXA1 has been predominantly studied for its binding to formyl peptide receptors (FPRs) on plasma membranes, little is known regarding whether this protein has an anti-inflammatory effect in the cytosol. Here, we investigated the mechanism by which the ANXA1 peptide Ac2-26 decreases high TNF-α production and IKKβ activity, which was caused by oxygen glucose deprivation/reperfusion (OGD/R)-induced neuronal conditioned medium (NCM) in microglia...
2018: Frontiers in Molecular Neuroscience
https://www.readbyqxmd.com/read/29662239/elimination-of-tdp-43-inclusions-linked-to-amyotrophic-lateral-sclerosis-by-a-misfolding-specific-intrabody-with-dual-proteolytic-signals
#8
Yoshitaka Tamaki, Akemi Shodai, Toshifumi Morimura, Ryota Hikiami, Sumio Minamiyama, Takashi Ayaki, Ikuo Tooyama, Yoshiaki Furukawa, Ryosuke Takahashi, Makoto Urushitani
Aggregation of TAR DNA-binding protein of 43 kDa (TDP-43) is implicated in the pathogenesis of sporadic and certain familial forms of amyotrophic lateral sclerosis (ALS), suggesting elimination of TDP-43 aggregates as a possible therapeutic strategy. Here we generated and investigated a single-chain variable fragment (scFv) derived from the 3B12A monoclonal antibody (MAb) that recognises D247 of the TDP-43 nuclear export signal, an epitope masked in the physiological state. In transfected HEK293A cells, 3B12A scFv recapitulated the affinity of the full-length MAb to mislocalised TDP-43 with a defective nuclear localising signal and to a TDP-43 inclusion mimic with cysteine-to-serine substitution at RRM1...
April 16, 2018: Scientific Reports
https://www.readbyqxmd.com/read/29662162/a-switch-point-in-the-molecular-chaperone-hsp90-responding-to-client-interaction
#9
Daniel Andreas Rutz, Qi Luo, Lee Freiburger, Tobias Madl, Ville R I Kaila, Michael Sattler, Johannes Buchner
Heat shock protein 90 (Hsp90) is a dimeric molecular chaperone that undergoes large conformational changes during its functional cycle. It has been established that conformational switch points exist in the N-terminal (Hsp90-N) and C-terminal (Hsp90-C) domains of Hsp90, however information for switch points in the large middle-domain (Hsp90-M) is scarce. Here we report on a tryptophan residue in Hsp90-M as a new type of switch point. Our study shows that this conserved tryptophan senses the interaction of Hsp90 with a stringent client protein and transfers this information via a cation-π interaction with a neighboring lysine...
April 16, 2018: Nature Communications
https://www.readbyqxmd.com/read/29662061/rpap3-provides-a-flexible-scaffold-for-coupling-hsp90-to-the-human-r2tp-co-chaperone-complex
#10
Fabrizio Martino, Mohinder Pal, Hugo Muñoz-Hernández, Carlos F Rodríguez, Rafael Núñez-Ramírez, David Gil-Carton, Gianluca Degliesposti, J Mark Skehel, S Mark Roe, Chrisostomos Prodromou, Laurence H Pearl, Oscar Llorca
The R2TP/Prefoldin-like co-chaperone, in concert with HSP90, facilitates assembly and cellular stability of RNA polymerase II, and complexes of PI3-kinase-like kinases such as mTOR. However, the mechanism by which this occurs is poorly understood. Here we use cryo-EM and biochemical studies on the human R2TP core (RUVBL1-RUVBL2-RPAP3-PIH1D1) which reveal the distinctive role of RPAP3, distinguishing metazoan R2TP from the smaller yeast equivalent. RPAP3 spans both faces of a single RUVBL ring, providing an extended scaffold that recruits clients and provides a flexible tether for HSP90...
April 16, 2018: Nature Communications
https://www.readbyqxmd.com/read/29661843/functional-analysis-of-hif1-histone-chaperone-in-saccharomyces-cerevisiae
#11
Nora S Dannah, Syed Nabeel-Shah, Christoph F Kurat, Sarah A Sabatinos, Jeffrey Fillingham
The Hif1 protein in the yeast Saccharomyces cerevisie is an evolutionarily conserved H3/H4-specific chaperone and a subunit of the nuclear Hat1 complex that catalyzes the acetylation of newly synthesized histone H4. Hif1, as well as its human homolog NASP, has been implicated in an array of chromatin-related processes including histone H3/H4 transport, chromatin assembly and DNA repair. In this study, we elucidate the functional aspects of Hif1. Initially we establish the wide distribution of Hif1 homologs with an evolutionarily conserved pattern of four tetratricopeptide repeats (TPR) motifs throughout the major fungal lineages and beyond...
April 16, 2018: G3: Genes—Genomes—Genetics
https://www.readbyqxmd.com/read/29661622/rational-design-and-screening-of-peptide-based-inhibitors-of-heat-shock-factor-1-hsf1
#12
Xu Ran, Eileen T Burchfiel, Bushu Dong, Nicholas J Rettko, Bryan M Dunyak, Hao Shao, Dennis J Thiele, Jason E Gestwicki
Heat shock factor 1 (HSF1) is a stress-responsive transcription factor that regulates expression of protein chaperones and cell survival factors. In cancer, HSF1 plays a unique role, hijacking the normal stress response to drive a cancer-specific transcriptional program. These observations suggest that HSF1 inhibitors could be promising therapeutics. However, HSF1 is activated through a complex mechanism, which involves release of a negative regulatory domain, leucine zipper 4 (LZ4), from a masked oligomerization domain (LZ1-3), and subsequent binding of the oligomer to heat shock elements (HSEs) in HSF1-responsive genes...
April 7, 2018: Bioorganic & Medicinal Chemistry
https://www.readbyqxmd.com/read/29660399/cacybp-sip-a-hsp90-binding-chaperone-in-cellular-stress-response
#13
Agnieszka Góral, Katarzyna Bartkowska, Rouzanna L Djavadian, Anna Filipek
CacyBP/SIP interacts with Hsp90 and is able to protect proteins from denaturation and/or aggregation induced by elevated temperature. In this work we studied the influence of different stress factors on CacyBP/SIP level in HEp-2 cells. We have found that H2 O2 and radicicol treatment resulted in a significant increase (up to 40-50%) in the CacyBP/SIP level. We have also found that HEp-2 cells overexpressing CacyBP/SIP were more resistant to stress-induced death. Further studies have revealed that the Hsf1 transcription factor binds to the CacyBP/SIP gene promoter and up-regulates CacyBP/SIP expression under stress conditions...
April 13, 2018: International Journal of Biochemistry & Cell Biology
https://www.readbyqxmd.com/read/29659649/systems-analysis-of-the-genetic-interaction-network-of-yeast-molecular-chaperones
#14
Kamran Rizzolo, Ashwani Kumar, Yoshito Kakihara, Sadhna Phanse, Zoran Minic, Jamie Snider, Igor Stagljar, Sandra Zilles, Mohan Babu, Walid A Houry
Molecular chaperones are typically promiscuous interacting proteins that function globally in the cell to maintain protein homeostasis. Recently, we had carried out experiments that elucidated a comprehensive interaction network for the core 67 chaperones and 15 cochaperones in the budding yeast Saccharomyces cerevisiae [Rizzolo et al., Cell Rep., 2017, 20, 2735-2748]. Here, the genetic (i.e. epistatic) interaction network obtained for chaperones was further analyzed, revealing that the global topological parameters of the resulting network have a more central role in mediating interactions in comparison to the rest of the proteins in the cell...
April 16, 2018: Molecular omics
https://www.readbyqxmd.com/read/29657945/the-role-of-protein-chaperones-in-the-survival-from-anthracycline-induced-oxidative-stress-in-saccharomyces-cerevisiae
#15
Jana S Miles, Samantha J Sojourner, Lahcen Jaafar, Aurellia Whitmore, Selina Darling-Reed, Hernan Flores-Rozas
Several S. cerevisiae deletion strains involving heat-shock response factors were among the most sensitive mutants identified in a previous genetic screen for doxorubicin hypersensitivity. These strains included ydj1Δ, ssz1Δ and zuo1Δ mutants. In addition, new1Δ , whose function was unknown, also displayed significant sensitivity to anthracyclines. We further investigated the basis for the sensitivity of these mutants. We determined that heat-shock could partially rescue the sensitivity of the strains to doxorubicin, including the homologous recombination mutant rad52Δ , which is sensitive to doxorubicin-mediated DNA double strand breaks (DSBs)...
March 2018: International Journal of Advanced Research
https://www.readbyqxmd.com/read/29651925/heptamer-peptide-disassembles-native-amyloid-in-human-plasma-via-heat-shock-protein-70
#16
Timothy James Cunningham, Jeffrey I Greenstein, Lihua Yao, Itzhak Fischer, Theresa Conners
Proteostasis, which includes the repair and disposal of misfolded proteins, depends in part on the activity of heat shock proteins, a well-known class of chaperone molecules. When this process fails abnormally folded proteins may accumulate in cells, tissues, and blood. These species are a hallmark of protein aggregation diseases but also amass during aging, often in the absence of an identified clinical disorder. We report that a neuroprotective cyclic heptapeptide, CHEC-7, which has been applied systemically as a therapeutic in animal neurodegeneration models, disrupts such aggregates and inhibits amyloidogenesis when added in nanomolar concentrations to human plasma...
April 13, 2018: Rejuvenation Research
https://www.readbyqxmd.com/read/29651044/yeast-aconitase-mitochondrial-import-is-modulated-by-interactions-of-its-c-and-n-terminal-domains-and-ssa1-2-hsp70
#17
Reut Ben-Menachem, Katherine Wang, Orly Marcu, Zhang Yu, Teck Kwang Lim, Qingsong Lin, Ora Schueler-Furman, Ophry Pines
Molecules of single proteins, echoforms, can be distributed between two (or more) subcellular locations, a phenomenon which we refer to as dual targeting or dual localization. The yeast aconitase gene ACO1 (778 amino acids), encodes a single translation product that is nonetheless dual localized to the cytosol and mitochondria by a reverse translocation mechanism. The solved crystal structure of aconitase isolated from porcine heart mitochondria shows that it has four domains. The first three tightly associated N-terminal domains are tethered to the larger C-terminal fourth domain (C-terminal amino acids 517-778)...
April 12, 2018: Scientific Reports
https://www.readbyqxmd.com/read/29650969/akaps-pka-disruptors-increase-aqp2-activity-independently-of-vasopressin-in-a-model-of-nephrogenic-diabetes-insipidus
#18
Fumiaki Ando, Shuichi Mori, Naofumi Yui, Tetsuji Morimoto, Naohiro Nomura, Eisei Sohara, Tatemitsu Rai, Sei Sasaki, Yoshiaki Kondo, Hiroyuki Kagechika, Shinichi Uchida
Congenital nephrogenic diabetes insipidus (NDI) is characterized by the inability of the kidney to concentrate urine. Congenital NDI is mainly caused by loss-of-function mutations in the vasopressin type 2 receptor (V2R), leading to impaired aquaporin-2 (AQP2) water channel activity. So far, treatment options of congenital NDI either by rescuing mutant V2R with chemical chaperones or by elevating cyclic adenosine monophosphate (cAMP) levels have failed to yield effective therapies. Here we show that inhibition of A-kinase anchoring proteins (AKAPs) binding to PKA increases PKA activity and activates AQP2 channels in cortical collecting duct cells...
April 12, 2018: Nature Communications
https://www.readbyqxmd.com/read/29650953/hsp27-is-a-partner-of-jak2-stat5-and-a-potential-therapeutic-target-in-myelofibrosis
#19
Margaux Sevin, Lucia Kubovcakova, Nicolas Pernet, Sébastien Causse, Franck Vitte, Jean Luc Villeval, Catherine Lacout, Marine Cordonnier, Fernando Rodrigues-Lima, Gaétan Chanteloup, Matthieu Mosca, Marie-Lorraine Chrétien, Jean Noël Bastie, Sylvain Audia, Paul Sagot, Selim Ramla, Laurent Martin, Martin Gleave, Valérie Mezger, Radek Skoda, Isabelle Plo, Carmen Garrido, François Girodon, Aurélie de Thonel
Heat shock protein 27 (HSP27/HSPB1) is a stress-inducible chaperone that facilitates cancer development by its proliferative and anti-apoptotic functions. The OGX-427 antisense oligonucleotide against HSP27 has been reported to be beneficial against idiopathic pulmonary fibrosis. Here we show that OGX-427 is effective in two murine models of thrombopoietin- and JAKV617F-induced myelofibrosis. OGX-427 limits disease progression and is associated with a reduction in spleen weight, in megakaryocyte expansion and, for the JAKV617F model, in fibrosis...
April 12, 2018: Nature Communications
https://www.readbyqxmd.com/read/29650757/conformational-flexibility-within-the-nascent-polypeptide-associated-complex-enables-its-interactions-with-structurally-diverse-client-proteins
#20
Esther M Martin, Matthew P Jackson, Martin Gamerdinger, Karina Gense, Theodoros K Karamanos, Julia R Humes, Elke Deuerling, Alison E Ashcroft, Sheena E Radford
As newly synthesized polypeptides emerge from the ribosome, it is crucial that they fold correctly. To prevent premature aggregation, nascent chains interact with chaperones that facilitate folding or prevent misfolding until protein synthesis is complete. Nascent polypeptide-associated complex (NAC) is a ribosome-associated chaperone important for protein homeostasis. However, how NAC binds its substrates remains unclear. Using native electrospray ionization MS (ESI MS), limited proteolysis, NMR and cross-linking, we analysed the conformational properties of NAC from Caenorhabditis elegans and studied its ability to bind proteins in different conformational states...
April 12, 2018: Journal of Biological Chemistry
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