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Proteostasis

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https://www.readbyqxmd.com/read/29149599/autophagosomal-content-profiling-reveals-an-lc3c-dependent-piecemeal-mitophagy-pathway
#1
François Le Guerroué, Franziska Eck, Jennifer Jung, Tatjana Starzetz, Michel Mittelbronn, Manuel Kaulich, Christian Behrends
Autophagy allows the degradation of cytosolic endogenous and exogenous material in the lysosome. Substrates are engulfed by double-membrane vesicles, coined autophagosomes, which subsequently fuse with lysosomes. Depending on the involvement of specific receptor proteins, autophagy occurs in a selective or nonselective manner. While this process is well understood at the level of bulky cargo such as mitochondria and bacteria, we know very little about individual proteins and protein complexes that are engulfed and degraded by autophagy...
November 16, 2017: Molecular Cell
https://www.readbyqxmd.com/read/29148236/emerging-roles-of-er-stress-in-the-aetiology-and-pathogenesis-of-alzheimer-s-disease
#2
REVIEW
Yannis Gerakis, Claudio Hetz
Alzheimer's disease (AD) is a progressive neurodegenerative disease characterized by synaptic dysfunction and accumulation of abnormal aggregates formed by amyloid-β peptides or phophorylated Tau proteins. Accumulating evidence suggests that alterations in the buffering capacity of the proteostasis network is a salient feature of AD. The endoplasmic reticulum (ER) is the main compartment involved in protein folding and secretion and is drastically affected in AD neurons. ER stress triggers the activation of the Unfolded Protein Response (UPR), a signal transduction pathway that enforces adaptive programs to recover homeostasis or trigger apoptosis of irreversibly damaged cells...
November 17, 2017: FEBS Journal
https://www.readbyqxmd.com/read/29147580/molecular-age-related-changes-in-the-anterior-segment-of-the-eye
#3
REVIEW
Luis Fernando Hernandez-Zimbron, Rosario Gulias-Cañizo, María F Golzarri, Blanca Elizabeth Martínez-Báez, Hugo Quiroz-Mercado, Roberto Gonzalez-Salinas
Purpose: To examine the current knowledge about the age-related processes in the anterior segment of the eye at a biological, clinical, and molecular level. Methods: We reviewed the available published literature that addresses the aging process of the anterior segment of the eye and its associated molecular and physiological events. We performed a search on PubMed, CINAHL, and Embase using the MeSH terms "eye," "anterior segment," and "age." We generated searches to account for synonyms of these keywords and MESH headings as follows: (1) "Eye" AND "ageing process" OR "anterior segment ageing" and (2) "Anterior segment" AND "ageing process" OR "anterior segment" AND "molecular changes" AND "age...
2017: Journal of Ophthalmology
https://www.readbyqxmd.com/read/29147466/erratum-to-resveratrol-attenuates-copper-induced-senescence-by-improving-cellular-proteostasis
#4
Liliana Matos, Alexandra Monteiro Gouveia, Henrique Almeida
[This corrects the article DOI: 10.1155/2017/3793817.].
2017: Oxidative Medicine and Cellular Longevity
https://www.readbyqxmd.com/read/29142280/mild-heat-induces-a-distinct-eustress-response-in-chinese-hamster-ovary-cells-but-does-not-induce-heat-shock-protein-synthesis
#5
Begüm Peksel, Imre Gombos, Mária Péter, László Vigh, Ádám Tiszlavicz, Mario Brameshuber, Gábor Balogh, Gerhard J Schütz, Ibolya Horváth, László Vigh, Zsolt Török
The current research on cellular heat stress management focuses on the roles of heat shock proteins (HSPs) and the proteostasis network under severe stress conditions. The mild, fever-type stress and the maintenance of membrane homeostasis are less well understood. Herein, we characterized the acute effect of mild, fever-range heat shock on membrane organization, and HSP synthesis and localization in two mammalian cell lines, to delineate the role of membranes in the sensing and adaptation to heat. A multidisciplinary approach combining ultrasensitive fluorescence microscopy and lipidomics revealed the molecular details of novel cellular "eustress", when cells adapt to mild heat by maintaining membrane homeostasis, activating lipid remodeling, and redistributing chaperone proteins...
November 15, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29138251/mitochondrial-inner-membrane-protease-yme1-degrades-outer-membrane-proteins-tom22-and-om45
#6
Xi Wu, Lanlan Li, Hui Jiang
Mitochondria are double-membraned organelles playing essential metabolic and signaling functions. The mitochondrial proteome is under surveillance by two proteolysis systems: the ubiquitin-proteasome system degrades mitochondrial outer-membrane (MOM) proteins, and the AAA proteases maintain the proteostasis of intramitochondrial compartments. We previously identified a Doa1-Cdc48(-Ufd1-Npl4) complex that retrogradely translocates ubiquitinated MOM proteins to the cytoplasm for degradation. In this study, we report the unexpected identification of MOM proteins whose degradation requires the Yme1(-Mgr1-Mgr3)i-AAA protease complex in mitochondrial inner membrane...
November 14, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/29135234/evaluating-the-effect-of-phosphorylation-on-the-structure-and-dynamics-of-hsp27-dimers-by-means-of-ion-mobility-mass-spectrometry
#7
Blagojce Jovcevski, Megan A Kelly, J Andrew Aquilina, Justin L P Benesch, Heath Ecroyd
The quaternary structure and dynamics of the human small heat-shock protein Hsp27 is linked to its molecular chaperone function and influenced by post-translational modifications, including phosphorylation. Phosphorylation of Hsp27 promotes oligomer dissociation and can enhance chaperone activity. This study explored the impact of phosphorylation on the quaternary structure and dynamics of Hsp27. Using mutations that mimic phosphorylation and ion mobility mass spectrometry we show that successive substitutions result in an increase in the conformational heterogeneity of Hsp27 dimers...
November 14, 2017: Analytical Chemistry
https://www.readbyqxmd.com/read/29132128/a-single-cysteine-post-translational-oxidation-suffices-to-compromise-globular-proteins-kinetic-stability-and-promote-amyloid-formation
#8
Patrizia Marinelli, Susanna Navarro, Ricardo Graña-Montes, Manuel Bañó-Polo, María Rosario Fernández, Elena Papaleo, Salvador Ventura
Oxidatively modified forms of proteins accumulate during aging. Oxidized protein conformers might act as intermediates in the formation of amyloids in age-related disorders. However, it is not known whether this amyloidogenic conversion requires an extensive protein oxidative damage or it can be promoted just by a discrete, localized post-translational modification of certain residues. Here, we demonstrate that the irreversible oxidation of a single free Cys suffices to severely perturb the folding energy landscape of a stable globular protein, compromise its kinetic stability, and lead to the formation of amyloids under physiological conditions...
October 31, 2017: Redox Biology
https://www.readbyqxmd.com/read/29127110/pathways-of-cellular-proteostasis-in-aging-and-disease
#9
REVIEW
Courtney L Klaips, Gopal Gunanathan Jayaraj, F Ulrich Hartl
Ensuring cellular protein homeostasis, or proteostasis, requires precise control of protein synthesis, folding, conformational maintenance, and degradation. A complex and adaptive proteostasis network coordinates these processes with molecular chaperones of different classes and their regulators functioning as major players. This network serves to ensure that cells have the proteins they need while minimizing misfolding or aggregation events that are hallmarks of age-associated proteinopathies, including neurodegenerative disorders such as Alzheimer's and Parkinson's diseases...
November 10, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/29117555/mitochondrial-stress-restores-the-heat-shock-response-and-prevents-proteostasis-collapse-during-aging
#10
Johnathan Labbadia, Renee M Brielmann, Mario F Neto, Yi-Fan Lin, Cole M Haynes, Richard I Morimoto
In Caenorhabditis elegans, the programmed repression of the heat shock response (HSR) accompanies the transition to reproductive maturity, leaving cells vulnerable to environmental stress and protein aggregation with age. To identify the factors driving this event, we performed an unbiased genetic screen for suppressors of stress resistance and identified the mitochondrial electron transport chain (ETC) as a central regulator of the age-related decline of the HSR and cytosolic proteostasis. Mild downregulation of ETC activity, either by genetic modulation or exposure to mitochondria-targeted xenobiotics, maintained the HSR in adulthood by increasing HSF-1 binding and RNA polymerase II recruitment at HSF-1 target genes...
November 7, 2017: Cell Reports
https://www.readbyqxmd.com/read/29113832/connecting-chaperone-mediated-autophagy-dysfunction-to-cellular-senescence
#11
REVIEW
Daniel Moreno-Blas, Elisa Gorostieta-Salas, Susana Castro-Obregón
Chaperone-mediated autophagy (CMA) is one of the main pathways of the lysosome-autophagy proteolytic system. It regulates different cellular process through the selective degradation of cytosolic proteins. In ageing, the function of CMA is impaired causing an inefficient stress response and the accumulation of damaged, oxidized or misfolded proteins, which is associated with numerous age-related diseases. Deficient protein degradation alters cellular proteostasis and activates signaling pathways that culminate in the induction of cellular senescence, whose accumulation is a typical feature of ageing...
November 4, 2017: Ageing Research Reviews
https://www.readbyqxmd.com/read/29111563/multiple-genes-contribute-to-anhydrobiosis-tolerance-to-extreme-desiccation-in-the-nematode-panagrolaimus-superbus
#12
Cláudia Carolina Silva Evangelista, Giovanna Vieira Guidelli, Gustavo Borges, Thais Fenz Araujo, Tiago Alves Jorge de Souza, Ubiraci Pereira da Costa Neves, Alan Tunnacliffe, Tiago Campos Pereira
The molecular basis of anhydrobiosis, the state of suspended animation entered by some species during extreme desiccation, is still poorly understood despite a number of transcriptome and proteome studies. We therefore conducted functional screening by RNA interference (RNAi) for genes involved in anhydrobiosis in the holo-anhydrobiotic nematode Panagrolaimus superbus. A new method of survival analysis, based on staining, and proof-of-principle RNAi experiments confirmed a role for genes involved in oxidative stress tolerance, while a novel medium-scale RNAi workflow identified a further 40 anhydrobiosis-associated genes, including several involved in proteostasis, DNA repair and signal transduction pathways...
November 6, 2017: Genetics and Molecular Biology
https://www.readbyqxmd.com/read/29110485/discovery-of-aromatic-carbamates-that-confer-neuroprotective-activity-by-enhancing-autophagy-and-inducing-the-anti-apoptotic-protein-b-cell-lymphoma-2-bcl-2
#13
Nihar Kinarivala, Ronak Patel, Rose-Mary Boustany, Abraham J Al-Ahmad, Paul C Trippier
Neurodegenerative diseases share certain pathophysiological hallmarks that represent common targets for drug discovery. In particular, dysfunction of proteostasis and the resultant apoptotic death of neurons, represent common pathways for pharmacological intervention. A library of aromatic carbamate derivatives based on the clinically available drug flupirtine was synthesized to determine a structure-activity relationship for neuroprotective activity. Several derivatives were identified that possess greater protective effect in human induced pluripotent stem cell-derived neurons, protecting up to 80% of neurons against etoposide-induced apoptosis at concentrations as low as 100 nM...
November 7, 2017: Journal of Medicinal Chemistry
https://www.readbyqxmd.com/read/29109084/ubiquitin-binding-protein-cg5445-suppresses-aggregation-and-cytotoxicity-of-amyotrophic-lateral-sclerosis-linked-tdp-43-in-drosophila
#14
Hiroyuki Uechi, Erina Kuranaga, Tomohiro Iriki, Kohei Takano, Shoshiro Hirayama, Masayuki Miura, Jun Hamazaki, Shigeo Murata
Ubiquitin-mediated protein degradation plays essential roles in proteostasis and is involved in the pathogenesis of neurodegenerative diseases in which ubiquitin-positive aberrant proteins accumulate. However, how such aberrant proteins are processed inside cells has not been fully explored. Here, we show that the product of CG5445, a previously uncharacterized Drosophila gene, prevents accumulation of aggregate-prone ubiquitinated proteins. We found that ubiquitin conjugates were associated with CG5445, knockdown of which caused accumulation of detergent-insoluble ubiquitinated proteins...
November 6, 2017: Molecular and Cellular Biology
https://www.readbyqxmd.com/read/29107797/establishment-of-a-de-novo-reference-transcriptome-of-histomonas-meleagridis-reveals-basic-insights-about-biological-functions-and-potential-pathogenic-mechanisms-of-the-parasite
#15
Rounik Mazumdar, Lukas Endler, Andreas Monoyios, Michael Hess, Ivana Bilic
The protozoan flagellate Histomonas meleagridis is the causative agent of histomonosis in poultry. In turkeys, high mortality might be noticed whereas in chickens the disease is less severe despite production losses. Discovered over a century ago, molecular data on this parasite are scarce and genetic studies are in its infancy. To expand genomic information, a de novo transcriptome sequencing of H. meleagridis was performed from a virulent and an attenuated strain, cultivated in vitro as monoxenic mono-eukaryotic culture...
October 6, 2017: Protist
https://www.readbyqxmd.com/read/29107503/abrogating-mitochondrial-dynamics-in-mouse-hearts-accelerates-mitochondrial-senescence
#16
Moshi Song, Antonietta Franco, Julie A Fleischer, Lihong Zhang, Gerald W Dorn
Mitochondrial fusion and fission are critical to heart health; genetically interrupting either is rapidly lethal. To understand whether it is loss of, or the imbalance between, fusion and fission that underlies observed cardiac phenotypes, we engineered mice in which Mfn-mediated fusion and Drp1-mediated fission could be concomitantly abolished. Compared to fusion-defective Mfn1/Mfn2 cardiac knockout or fission-defective Drp1 cardiac knockout mice, Mfn1/Mfn2/Drp1 cardiac triple-knockout mice survived longer and manifested a unique pathological form of cardiac hypertrophy...
October 21, 2017: Cell Metabolism
https://www.readbyqxmd.com/read/29107114/cancer-chemoprevention-via-activation-of-proteostatic-modules
#17
Aimilia Sklirou, Eleni-Dimitra Papanagnou, Nikolas Fokialakis, Ioannis P Trougakos
Proteins carry out the majority of cellular functions and maintain cellular homeodynamics mostly by participating in multimeric assemblies that operate as protein machines. Proteome quality control is thus critical for cellular functionality, and it is carried out through the curating activity of the proteostasis network (PN). Key components of the PN are the protein synthesis and trafficking modules, the endoplasmic reticulum unfolded protein response, molecular chaperones, and the two main degradation machineries, namely the ubiquitin proteasome and autophagy lysosome pathways...
October 26, 2017: Cancer Letters
https://www.readbyqxmd.com/read/29106597/thermophilic-adaptation-in-prokaryotes-is-constrained-by-metabolic-costs-of-proteostasis
#18
Sergey V Venev, Konstantin B Zeldovich
Prokaryotes evolved to thrive in an extremely diverse set of habitats, and their proteomes bear signatures of environmental conditions. Although correlations between amino acid usage and environmental temperature are well documented, understanding of the mechanisms of thermal adaptation remains incomplete. Here, we couple the energetic costs of protein folding and protein homeostasis to build a microscopic model explaining both the overall amino acid composition and its temperature trends. Low biosynthesis costs lead to low diversity of physical interactions between amino acid residues, which in turn makes proteins less stable and drives up chaperone activity to maintain appropriate levels of folded, functional proteins...
November 2, 2017: Molecular Biology and Evolution
https://www.readbyqxmd.com/read/29103937/an-intracellular-pathogen-response-pathway-promotes-proteostasis-in-c-%C3%A2-elegans
#19
Kirthi C Reddy, Tal Dror, Jessica N Sowa, Johan Panek, Kevin Chen, Efrem S Lim, David Wang, Emily R Troemel
Maintenance of protein homeostasis, or proteostasis, is crucial for organismal health. Disruption of proteostasis can lead to the accumulation of protein aggregates, which are associated with aging and many human diseases such as Alzheimer's disease [1-3]. Through analysis of the C. elegans host response to intracellular infection, we describe here a novel response pathway that enhances proteostasis capacity and appears to act in parallel to well-studied proteostasis pathways. These findings are based on analysis of the transcriptional response to infection by the intracellular pathogen Nematocida parisii [4]...
October 30, 2017: Current Biology: CB
https://www.readbyqxmd.com/read/29100054/systems-phytohormone-responses-to-mitochondrial-proteotoxic-stress
#20
Xu Wang, Johan Auwerx
Mitochondrial function is controlled by two separate genomes. This feature makes mitochondria prone to proteotoxic stress when a stoichiometric imbalance occurs in the protein complexes that perform oxidative phosphorylation, which consist of both nuclear- and mitochondrial-encoded proteins. Such a proteotoxic stress is known to induce the mitochondrial unfolded protein response (UPR(mt)) in animals. It is unknown whether UPR(mt) occurs in plants. Here, we induced a mitonuclear protein imbalance in Arabidopsis through chemical or genetic interference...
November 2, 2017: Molecular Cell
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