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https://www.readbyqxmd.com/read/29346421/the-absence-of-specific-yeast-heat-shock-proteins-leads-to-abnormal-aggregation-and-compromised-autophagic-clearance-of-mutant-huntingtin-proteins
#1
Ryan Higgins, Marie-Helene Kabbaj, Alexa Hatcher, Yanchang Wang
The functionality of a protein depends on its correct folding, but newly synthesized proteins are susceptible to aberrant folding and aggregation. Heat shock proteins (HSPs) function as molecular chaperones that aid in protein folding and the degradation of misfolded proteins. Trinucleotide (CAG) repeat expansion in the Huntingtin gene (HTT) results in the expression of misfolded Huntingtin protein (Htt), which contributes to the development of Huntington's disease. We previously found that the degradation of mutated Htt with polyQ expansion (Htt103QP) depends on both ubiquitin proteasome system and autophagy...
2018: PloS One
https://www.readbyqxmd.com/read/29345620/functional-role-of-the-type-1-pilus-rod-structure-in-mediating-host-pathogen-interactions
#2
Caitlin N Spaulding, Henry Louis Schreiber, Weili Zheng, Karen W Dodson, Jennie E Hazen, Matt S Conover, Fengbin Wang, Pontus Svenmarker, Areli Luna-Rico, Olivera Francetic, Magnus Andersson, Scott Hultgren, Edward H Egelman
Uropathogenic E. coli (UPEC), which cause urinary tract infections (UTI), utilize type 1 pili, a chaperone usher pathway (CUP) pilus, to cause UTI and colonize the gut. The pilus rod, comprised of repeating FimA subunits, provides a structural scaffold for displaying the tip adhesin, FimH. We solved the 4.2 Å resolution structure of the type 1 pilus rod using cryo-electron microscopy. Residues forming the interactive surfaces that determine the mechanical properties of the rod were maintained by selection based on a global alignment of fimA sequences...
January 18, 2018: ELife
https://www.readbyqxmd.com/read/29343244/hsp70-at-the-membrane-driving-protein-translocation
#3
REVIEW
Elizabeth A Craig
Efficient movement of proteins across membranes is required for cell health. The translocation process is particularly challenging when the channel in the membrane through which proteins must pass is narrow-such as those in the membranes of the endoplasmic reticulum and mitochondria. Hsp70 molecular chaperones play roles on both sides of these membranes, ensuring efficient translocation of proteins synthesized on cytosolic ribosomes into the interior of these organelles. The "import motor" in the mitochondrial matrix, which is essential for driving the movement of proteins across the mitochondrial inner membrane, is arguably the most complex Hsp70-based system in the cell...
January 17, 2018: BMC Biology
https://www.readbyqxmd.com/read/29342862/heterogeneous-contributing-factors-in-mpm-disease-development-and-progression-biological-advances-and-clinical-implications
#4
REVIEW
Bhairavi Tolani, Luis A Acevedo, Ngoc T Hoang, Biao He
Malignant pleural mesothelioma (MPM) tumors are remarkably aggressive and most patients only survive for 5-12 months; irrespective of stage; after primary symptoms appear. Compounding matters is that MPM remains unresponsive to conventional standards of care; including radiation and chemotherapy. Currently; instead of relying on molecular signatures and histological typing; MPM treatment options are guided by clinical stage and patient characteristics because the mechanism of carcinogenesis has not been fully elucidated; although about 80% of cases can be linked to asbestos exposure...
January 13, 2018: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/29339390/identification-of-hsp90-inhibitors-with-anti-plasmodium-activity
#5
Dora Posfai, Amber L Eubanks, Allison I Keim, Kuan-Yi Lu, Grace Z Wang, Philip F Hughes, Nobutaka Kato, Timothy A Haystead, Emily R Derbyshire
Malaria remains a global health burden partly due to Plasmodium parasite resistance to first-line therapeutics. The molecular chaperone heat shock protein 90 (Hsp90) has emerged as an essential protein for blood stage Plasmodium parasites, but details about its function during malaria's elusive liver stage are unclear. We used target-based screens to identify compounds that bind to Plasmodium falciparum and human Hsp90, which revealed insights into chemotypes with species selective binding. Using cell-based malaria assays, we demonstrate that all identified Hsp90-binding compounds are liver and blood stage Plasmodium inhibitors...
January 16, 2018: Antimicrobial Agents and Chemotherapy
https://www.readbyqxmd.com/read/29339381/cholecystokinin-is-involved-in-triglyceride-fatty-acid-uptake-by-rat-adipose-tissue
#6
Adrian Plaza, Beatriz Merino, Victoria Cano, Gema Domínguez, Javier Pérez-Castells, Maria S Fernandez-Alfonso, Coralie Sengenès, Julie A Chowen, Mariano Ruiz-Gayo
The incorporation of plasma triglyceride (TG) fatty acids to white adipose tissue (WAT) depends on lipoprotein lipase (LPL), which is regulated by angiopoietin-like protein-4 (ANGPTL-4), an unfolding molecular chaperone that converts active LPL dimers into inactive monomers. The production of ANGPTL-4 is promoted by fasting and repressed by feeding. We hypothesized that the postprandial hormone cholecystokinin (CCK) facilitates the storage of dietary TG fatty acids in WAT by regulating the activity of the LPL/ANGPTL-4 axis and that it does so by acting directly on CCK receptors in adipocytes...
January 16, 2018: Journal of Endocrinology
https://www.readbyqxmd.com/read/29339092/structural-and-biochemical-analyses-reveal-ubiquitin-c-terminal-hydrolase-l1-as-a-specific-client-of-the-peroxiredoxin-ii-chaperone
#7
Sang Pil Lee, Chan Mi Park, Kyung Seok Kim, Eunji Kim, Moonkyung Jeong, Ji-Young Shin, Chul-Ho Yun, Kanghwa Kim, P Boon Chock, Ho Zoon Chae
Peroxiredoxins (Prxs) play dual roles as both thiol-peroxidases and molecular chaperones. Peroxidase activity enables various intracellular functions, however, the physiological roles of Prxs as chaperones are not well established. To study the chaperoning function of Prx, we previously sought to identify heat-induced Prx-binding proteins as the clients of a Prx chaperone. By using His-tagged Prx I as a bait, we separated ubiquitin C-terminal hydrolase-L1 (UCH-L1) as a heat-induced Prx I binding protein from rat brain crude extracts...
January 12, 2018: Archives of Biochemistry and Biophysics
https://www.readbyqxmd.com/read/29337690/molecular-determinants-of-drosophila-immunophilin-fkbp39-nuclear-localization
#8
Marek Orłowski, Katarzyna Popławska, Joanna Pieprzyk, Aleksandra Szczygieł-Sommer, Anna Więch, Mirosław Zarębski, Aneta Tarczewska, Jurek Dobrucki, Andrzej Ożyhar
FK506-binding proteins (FKBPs) belong to a distinct class of immunophilins that interact with immunosuppressants. They use their peptidyl-prolyl isomerase (PPIase) activity to catalyse the cis-trans conversion of prolyl bonds in proteins during protein-folding events. FKBPs also act as a unique group of chaperones. The Drosophila melanogaster peptidylprolyl cis-trans isomerase FK506-binding protein of 39 kDa (FKBP39) is thought to act as a transcriptional modulator of gene expression in 20-hydroxyecdysone and juvenile hormone signal transduction...
June 27, 2017: Biological Chemistry
https://www.readbyqxmd.com/read/29334418/antimicrobial-and-stress-responses-to-increased-temperature-and-bacterial-pathogen-challenge-in-the-holobiont-of-a-reef-building-coral
#9
Jeroen A J M van de Water, Maryam Chaib De Mares, Groves B Dixon, Jean-Baptiste Raina, Bette L Willis, David G Bourne, Madeleine J H van Oppen
Global increases in coral disease prevalence have been linked to ocean warming through changes in coral-associated bacterial communities, pathogen virulence and immune system function. However, the interactive effects of temperature and pathogens on the coral holobiont are poorly understood. Here, we assessed three compartments of the holobiont (host, Symbiodinium, bacterial community) of the coral Montipora aequituberculata challenged with the pathogen Vibrio coralliilyticus and the commensal bacterium Oceanospirillales sp...
January 15, 2018: Molecular Ecology
https://www.readbyqxmd.com/read/29331340/hsp72-protects-from-liver-injury-via-attenuation-of-hepatocellular-death-oxidative-stress-and-jnk-signaling
#10
Kateryna Levada, Nurdan Guldiken, Xiaoji Zhang, Giovanna Vella, Fa-Rong Mo, Laura P James, Johannes Haybaeck, Sonja M Kessler, Alexandra K Kiemer, Thomas Ott, Daniel Hartmann, Norbert Hüser, Marianne Ziol, Christian Trautwein, Pavel Strnad
BACKGROUND AND AIMS: Heat shock protein (Hsp) 72 is a molecular chaperone that is upregulated in response to stress and possesses broad cytoprotective functions. To determine its hepatic function, we studied its expression in human liver disorders and its biological significance in newly generated transgenic animals. AIM AND METHODS: Double transgenic mice overexpressing Hsp72 (gene HSPA1A) under the control of a tissue-specific tetracycline-inducible system (Hsp72-LAP mice) were produced...
January 10, 2018: Journal of Hepatology
https://www.readbyqxmd.com/read/29328475/heat-shock-protein-27-knockdown-using-nucleotide%C3%A2-based-therapies-enhances-sensitivity-to-5-fu-chemotherapy-in-sw480-human-colon-cancer-cells
#11
Takehiro Shimada, Masashi Tsuruta, Hirotoshi Hasegawa, Koji Okabayashi, Kohei Shigeta, Takashi Ishida, Yusuke Asada, Hirofumi Suzumura, Kaoru Koishikawa, Shingo Akimoto, Yuko Kitagawa
Heat shock protein 27 (Hsp27) is a chaperone protein of low molecular weight that is produced in response to various stresses and has a cytoprotective function. In the present study we found that there is a strong correlation between sensitivity to 5-fluorouracil (5-FU) and the expression of Hsp27 in colorectal cancer. Apatorsen is an antisense oligonucleotide that targets Hsp27 and has various antitumor effects in some types of cancer, such as bladder and prostate. Although several clinical studies are currently studying apatorsen in many malignancies, to date no promising results have been reported for colorectal cancer...
January 3, 2018: Oncology Reports
https://www.readbyqxmd.com/read/29325094/functional-rescue-of-misfolding-abca3-mutations-by-small-molecular-correctors
#12
Susanna Kinting, Stefanie Höppner, Ulrike Schindlbeck, Maria E Forstner, Jacqueline Harfst, Thomas Wittmann, Matthias Griese
ABCA3, a phospholipid transporter in lung lamellar bodies (LB), is essential for the assembly of pulmonary surfactant and LB biogenesis. Mutations in the ABCA3 gene are an important genetic cause for respiratory distress syndrome in neonates and interstitial lung disease in children and adults, for which there is currently no cure.The aim of this study was to prove that disease causing misfolding ABCA3 mutations can be corrected in vitro and to investigate available options for correction.We stably expressed HA-tagged wild type ABCA3 or variants p...
January 9, 2018: Human Molecular Genetics
https://www.readbyqxmd.com/read/29323281/bap-sil1-regulates-the-molecular-chaperone-bip-by-coupling-release-of-nucleotide-and-substrate
#13
Mathias Rosam, Daniela Krader, Christina Nickels, Janine Hochmair, Katrin C Back, Ganesh Agam, Anders Barth, Cathleen Zeymer, Jelle Hendrix, Markus Schneider, Iris Antes, Jochen Reinstein, Don C Lamb, Johannes Buchner
BiP is the endoplasmic member of the Hsp70 family. BiP is regulated by several co-chaperones including the nucleotide-exchange factor (NEF) Bap (Sil1 in yeast). Bap is a two-domain protein. The interaction of the Bap C-terminal domain with the BiP ATPase domain is sufficient for its weak NEF activity. However, stimulation of the BiP ATPase activity requires full-length Bap, suggesting a complex interplay of these two factors. Here, single-molecule FRET experiments with mammalian proteins reveal that Bap affects the conformation of both BiP domains, including the lid subdomain, which is important for substrate binding...
January 2018: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/29323280/nucleotide-exchange-factors-fes1-and-hspbp1-mimic-substrate-to-release-misfolded-proteins-from-hsp70
#14
Naveen K C Gowda, Jayasankar M Kaimal, Roman Kityk, Chammiran Daniel, Jobst Liebau, Marie Öhman, Matthias P Mayer, Claes Andréasson
Protein quality control depends on the tight regulation of interactions between molecular chaperones and polypeptide substrates. Substrate release from the chaperone Hsp70 is triggered by nucleotide-exchange factors (NEFs) that control folding and degradation fates via poorly understood mechanisms. We found that the armadillo-type NEFs budding yeast Fes1 and its human homolog HspBP1 employ flexible N-terminal release domains (RDs) with substrate-mimicking properties to ensure the efficient release of persistent substrates from Hsp70...
January 2018: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/29320819/molecular-and-biochemical-characterization-of-opisthorchis-viverrini-calreticulin
#15
Wanlapa Chaibangyang, Amornrat Geadkaew-Krenc, Suksiri Vichasri-Grams, Smarn Tesana, Rudi Grams
Calreticulin (CALR), a multifunctional protein thoroughly researched in mammals, comprises N-, P-, and C-domain and has roles in calcium homeostasis, chaperoning, clearance of apoptotic cells, cell adhesion, and also angiogenesis. In this study, the spatial and temporal expression patterns of the Opisthorchis viverrini CALR gene were analyzed, and calcium-binding and chaperoning properties of recombinant O. viverrini CALR (OvCALR) investigated. OvCALR mRNA was detected from the newly excysted juvenile to the mature parasite by RT-PCR while specific antibodies showed a wide distribution of the protein...
December 2017: Korean Journal of Parasitology
https://www.readbyqxmd.com/read/29320742/defective-mitochondrial-trna-taurine-modification-activates-global-proteostress-and-leads-to-mitochondrial-disease
#16
Md Fakruddin, Fan-Yan Wei, Takeo Suzuki, Kana Asano, Takashi Kaieda, Akiko Omori, Ryoma Izumi, Atsushi Fujimura, Taku Kaitsuka, Keishi Miyata, Kimi Araki, Yuichi Oike, Luca Scorrano, Tsutomu Suzuki, Kazuhito Tomizawa
A subset of mitochondrial tRNAs (mt-tRNAs) contains taurine-derived modifications at 34U of the anticodon. Loss of taurine modification has been linked to the development of mitochondrial diseases, but the molecular mechanism is still unclear. Here, we showed that taurine modification is catalyzed by mitochondrial optimization 1 (Mto1) in mammals. Mto1 deficiency severely impaired mitochondrial translation and respiratory activity. Moreover, Mto1-deficient cells exhibited abnormal mitochondrial morphology owing to aberrant trafficking of nuclear DNA-encoded mitochondrial proteins, including Opa1...
January 9, 2018: Cell Reports
https://www.readbyqxmd.com/read/29320629/the-structural-asymmetry-of-mitochondrial-hsp90-trap1-determines-fine-tuning-of-functional-dynamics
#17
Elisabetta Moroni, David A Agard, Giorgio Colombo
The Hsp90 family of molecular chaperones oversees the folding of a wide range of client proteins. Hsp90 is a homodimer, whose conformational states and functions are regulated by ATP-binding and hydrolysis. The crystal structure of mitochondrial Hsp90 (Trap1) showed that one of the two protomers in the active state is buckled, resulting in an asymmetric conformation. The asymmetry between the two protomers corresponds to the broadly conserved region responsible for client binding. Moreover, asymmetry determines differential hydrolysis for each protomer, with the buckled conformation favoring ATP processing...
January 10, 2018: Journal of Chemical Theory and Computation
https://www.readbyqxmd.com/read/29317501/most-mutations-that-cause-spinocerebellar-ataxia-autosomal-recessive-type-16-scar16-destabilize-the-protein-quality-control-e3-ligase-chip
#18
Adam J Kanack, Oliver J Newsom, Kenneth Matthew Scaglione
The accumulation of misfolded proteins promotes protein aggregation and neuronal death in many neurodegenerative diseases. To counteract misfolded protein accumulation, neurons have pathways that recognize and refold or degrade aggregation-prone proteins. One U-box containing E3 ligase, C terminus of Hsc70-interacting protein (CHIP) plays a key role in this process, targeting misfolded proteins for proteasomal degradation. CHIP plays a protective role in mouse models of neurodegenerative disease, and in humans, mutations in CHIP cause spinocerebellar ataxia autosomal recessive type 16 (SCAR16), a fatal neurodegenerative disease characterized by truncal and limb ataxia that result in gait instability...
January 9, 2018: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29311085/the-rim-pathway-mediates-antifungal-tolerance-in-candida-albicans-through-newly-identified-rim101-transcriptional-targets-including-hsp90-and-ipt1
#19
Cécile Garnaud, Encar García-Oliver, Yan Wang, Danièle Maubon, Sébastien Bailly, Quentin Despinasse, Morgane Champleboux, Jérôme Govin, Muriel Cornet
Invasive candidiasis (IC) is a major cause of morbidity and mortality despite antifungal treatment. Azoles and echinocandins are used as first-line therapies in IC. However, their efficacy is limited by yeast tolerance and the emergence of acquired resistance. Tolerance is a reversible stage due to the yeast's capacity to counter the antifungal drug exposure, leading to persistent growth. In C. albicans, multiple stress signaling pathways have been shown to contribute to this adaptation. Among those, the Rim pH-responsive pathway, through its transcription factor Rim101p, was shown to mediate azole and echinocandin tolerance...
January 8, 2018: Antimicrobial Agents and Chemotherapy
https://www.readbyqxmd.com/read/29305010/histone-variants-and-disease
#20
Delphine Quénet
In eukaryotes, the genome is organized into a complex nucleoprotein structure called chromatin. Despite the simplicity of its monomer, DNA and two copies of four histones, the existence of histone variants opens possibilities of multiple chromatin landscapes and fine-tune regulation of molecular mechanisms for the regulation of gene expression and maintenance of genome stability. However, any defects in these combinations may contribute to disease development and/or progression. Here, I review human histone variants and their chaperones, and discuss how they contribute to pathological conditions...
2018: International Review of Cell and Molecular Biology
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