Cellular Stress Response
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Cellular Stress Response Pathways and Ageing: Intricate Molecular Relationships
The EMBO Journal (2011) 30, 2520–2531 | & 2011 European Molecular Biology Organization | All Rights Reserved 0261-4189/11 www.embojournal.org TTHEH E EEMBOMBO JJOURNALOURN AL EMBO Member’s Review Cellular stress response pathways and ageing: intricate molecular relationships Nikos Kourtis and Nektarios Tavernarakis* Over the past 20 years, ageing research has culminated in the identification of classical signalling pathways that Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, Heraklion, Crete, Greece influence ageing in a variety of species (Kenyon, 2010). Accumulating findings indicate that longevity depends on Ageing is driven by the inexorable and stochastic accumu- the ability of the organism to cope with extrinsic or intrinsic lation of damage in biomolecules vital for proper cellular stressors (Kirkwood and Austad, 2000). Indeed, compro- function. Although this process is fundamentally haph- mised stress responses are linked to the onset of many age- azard and uncontrollable, senescent decline and ageing related diseases.‘Stress’ is broadly defined as a noxious factor is broadly influenced by genetic and extrinsic factors. (physical, chemical or biological), which triggers a series of Numerous gene mutations and treatments have been cellular and systemic events, resulting in restoration of shown to extend the lifespan of diverse organisms ranging cellular and organismal homeostasis. To cope with conditions from the unicellular Saccharomyces cerevisiae to primates. of stress, organisms -
Ubiquitination Is Essential for Recovery of Cellular Activities Following Heat Shock Authors: Brian A
bioRxiv preprint doi: https://doi.org/10.1101/2021.04.22.440934; this version posted April 22, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made availableS ubmittedunder aCC-BY-NC-ND Manuscript: 4.0 Confidential International license. Ubiquitination is essential for recovery of cellular activities following heat shock Authors: Brian A. Maxwell1, Youngdae Gwon1, Ashutosh Mishra2, Junmin Peng2, Ke Zhang3, 5 Hong Joo Kim1 and J. Paul Taylor1,4* Affiliations: 1Department of Cell and Molecular Biology, St. Jude Children’s Research Hospital, Memphis, TN, USA 10 2Department of Structural Biology Department, St. Jude Children’s Research Hospital, Memphis, TN, USA 3Department of Neuroscience, Mayo Clinic Florida, Jacksonville, FL 32224 4Howard Hughes Medical Institute, Chevy Chase, MD 20815 *Correspondence to: [email protected] 15 Abstract: Eukaryotic cells respond to stress via adaptive programs that include reversible shutdown of key cellular processes, the formation of stress granules, and a global increase in ubiquitination. The primary function of this ubiquitination is generally considered to be tagging damaged or 20 misfolded proteins for degradation. Here we show that different types of stress generate distinct ubiquitination patterns. For heat stress, ubiquitination correlates with cellular activities that are downregulated during stress, including nucleocytoplasmic transport and translation, as well as with stress granule constituents. Ubiquitination is not required for the shutdown of these processes or for stress granule formation, but is essential for resumption of cellular activities and 25 for stress granule disassembly. -
Cellular Stress Responses: Cell Survival and Cell Death
Hindawi Publishing Corporation International Journal of Cell Biology Volume 2010, Article ID 214074, 23 pages doi:10.1155/2010/214074 Review Article Cellular Stress Responses: Cell Survival and Cell Death Simone Fulda,1 Adrienne M. Gorman,2 Osamu Hori,3 and Afshin Samali2 1 Children’s Hospital, Ulm University, Eythstraße. 24, 89075 Ulm, Germany 2 School of Natural Sciences, National University of Ireland, Galway, University Road, Galway, Ireland 3 Kanazawa University Graduate School of Medical Science, Department of Neuroanatomy, Kanazawa City, Ishikawa, 920-8640 Japan, Japan Correspondence should be addressed to Simone Fulda, [email protected] Received 4 August 2009; Accepted 20 November 2009 Academic Editor: Srinivasa M. Srinivasula Copyright © 2010 Simone Fulda et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Cells can respond to stress in various ways ranging from the activation of survival pathways to the initiation of cell death that eventually eliminates damaged cells. Whether cells mount a protective or destructive stress response depends to a large extent on the nature and duration of the stress as well as the cell type. Also, there is often the interplay between these responses that ultimately determines the fate of the stressed cell. The mechanism by which a cell dies (i.e., apoptosis, necrosis, pyroptosis, or autophagic cell death) depends on various exogenous factors as well as the cell’s ability to handle the stress to which it is exposed. The implications of cellular stress responses to human physiology and diseases are manifold and will be discussed in this review in the context of some major world health issues such as diabetes, Parkinson’s disease, myocardial infarction, and cancer. -
Review Article Cellular Stress Responses: Cell Survival and Cell Death
Hindawi Publishing Corporation International Journal of Cell Biology Volume 2010, Article ID 214074, 23 pages doi:10.1155/2010/214074 Review Article Cellular Stress Responses: Cell Survival and Cell Death Simone Fulda,1 Adrienne M. Gorman,2 Osamu Hori,3 and Afshin Samali2 1 Children’s Hospital, Ulm University, Eythstraße. 24, 89075 Ulm, Germany 2 School of Natural Sciences, National University of Ireland, Galway, University Road, Galway, Ireland 3 Kanazawa University Graduate School of Medical Science, Department of Neuroanatomy, Kanazawa City, Ishikawa, 920-8640 Japan, Japan Correspondence should be addressed to Simone Fulda, [email protected] Received 4 August 2009; Accepted 20 November 2009 Academic Editor: Srinivasa M. Srinivasula Copyright © 2010 Simone Fulda et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Cells can respond to stress in various ways ranging from the activation of survival pathways to the initiation of cell death that eventually eliminates damaged cells. Whether cells mount a protective or destructive stress response depends to a large extent on the nature and duration of the stress as well as the cell type. Also, there is often the interplay between these responses that ultimately determines the fate of the stressed cell. The mechanism by which a cell dies (i.e., apoptosis, necrosis, pyroptosis, or autophagic cell death) depends on various exogenous factors as well as the cell’s ability to handle the stress to which it is exposed. The implications of cellular stress responses to human physiology and diseases are manifold and will be discussed in this review in the context of some major world health issues such as diabetes, Parkinson’s disease, myocardial infarction, and cancer. -
HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity
cells Review HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity 1, 2, 3, Thomas L. Prince y , Benjamin J. Lang y , Martin E. Guerrero-Gimenez y , Juan Manuel Fernandez-Muñoz 3 , Andrew Ackerman 1 and Stuart K. Calderwood 2,* 1 Department of Molecular Functional Genomics, Geisinger Clinic, Danville, PA 17821, USA 2 Department of Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02115, USA 3 Laboratory of Oncology, Institute of Medicine and Experimental Biology of Cuyo (IMBECU), National Scientific and Technical Research Council (CONICET), Buenos Aires B1657, Argentina * Correspondence: [email protected]; Tel.: +1-617-667-4240 These authors contributed equally to this work. y Received: 25 March 2020; Accepted: 19 April 2020; Published: 22 April 2020 Abstract: Heat shock factor 1 (HSF1) is the primary component for initiation of the powerful heat shock response (HSR) in eukaryotes. The HSR is an evolutionarily conserved mechanism for responding to proteotoxic stress and involves the rapid expression of heat shock protein (HSP) molecular chaperones that promote cell viability by facilitating proteostasis. HSF1 activity is amplified in many tumor contexts in a manner that resembles a chronic state of stress, characterized by high levels of HSP gene expression as well as HSF1-mediated non-HSP gene regulation. HSF1 and its gene targets are essential for tumorigenesis across several experimental tumor models, and facilitate metastatic and resistant properties within cancer cells. Recent studies have suggested the significant potential of HSF1 as a therapeutic target and have motivated research efforts to understand the mechanisms of HSF1 regulation and develop methods for pharmacological intervention. -
Adaptive Posttranslational Control in Cellular Stress Response Pathways and Its Relationship to Toxicity
TOXICOLOGICAL SCIENCES, 147(2), 2015, 302–316 doi: 10.1093/toxsci/kfv130 Contemporary Review CONTEMPORARY REVIEW Adaptive Posttranslational Control in Cellular Stress Response Pathways and Its Relationship to Toxicity Testing and Safety Assessment Downloaded from Qiang Zhang,*,1 Sudin Bhattacharya,* Jingbo Pi,† Rebecca A. Clewell,* Paul L. Carmichael,‡ and Melvin E. Andersen* *Institute for Chemical Safety Sciences, The Hamner Institutes for Health Sciences, Research Triangle Park, http://toxsci.oxfordjournals.org/ North Carolina 27709; †School of Public Health, China Medical University, Shenyang, China; and ‡Unilever, Safety and Environmental Assurance Centre, Colworth Science Park, Sharnbrook, Bedfordshire, UK 1To whom correspondence should be addressed at Institute for Chemical Safety Sciences, The Hamner Institutes for Health Sciences, Research Triangle Park, North Carolina 27709. Fax: 1-919-558-1300. E-mail: [email protected] ABSTRACT at CIIT Library on September 25, 2015 Although transcriptional induction of stress genes constitutes a major cellular defense program against a variety of stressors, posttranslational control directly regulating the activities of preexisting stress proteins provides a faster-acting alternative response. We propose that posttranslational control is a general adaptive mechanism operating in many stress pathways. Here with the aid of computational models, we first show that posttranslational control fulfills two roles: (1) handling small, transient stresses quickly and (2) stabilizing the negative feedback transcriptional network. We then review the posttranslational control pathways for major stress responses—oxidative stress, metal stress, hyperosmotic stress, DNA damage, heat shock, and hypoxia. Posttranslational regulation of stress protein activities occurs by reversible covalent modifications, allosteric or non-allosteric enzymatic regulations, and physically induced protein structural changes. -
Variation in the Heat Shock Response and Its Implication for Predicting The
971 The Journal of Experimental Biology 213, 971-979 © 2010. Published by The Company of Biologists Ltd doi:10.1242/jeb.038034 Variation in the heat shock response and its implication for predicting the effect of global climate change on species’ biogeographical distribution ranges and metabolic costs L. Tomanek Center for Coastal Marine Sciences and Environmental Proteomics Laboratory, Department of Biological Sciences, California Polytechnic State University, San Luis Obispo, CA 93407, USA [email protected] Accepted 23 November 2009 Summary The preferential synthesis of heat shock proteins (Hsps) in response to thermal stress [the heat shock response (HSR)] has been shown to vary in species that occupy different thermal environments. A survey of case studies of aquatic (mostly marine) organisms occupying stable thermal environments at all latitudes, from polar to tropical, shows that they do not in general respond to heat stress with an inducible HSR. Organisms that occupy highly variable thermal environments (variations up to >20°C), like the intertidal zone, induce the HSR frequently and within the range of body temperatures they normally experience, suggesting that the response is part of their biochemical strategy to occupy this thermal niche. The highest temperatures at which these organisms can synthesize Hsps are only a few degrees Celsius higher than the highest body temperatures they experience. Thus, they live close to their thermal limits and any further increase in temperature is probably going to push them beyond those limits. In comparison, organisms occupying moderately variable thermal environments (<10°C), like the subtidal zone, activate the HSR at temperatures above those they normally experience in their habitats. -
Heat Shock Proteins & the Cellular Stress Response
Heat Shock Proteins & the Cellular Stress Response HSP90 & Co-Chaperones HSP70/HSP40 Chaperones HSP60/HSP10 (The Chaperonins) Small HSP & Crystallin Proteins Other Chaperones & Stress Proteins www.enzolifesciences.com Enabling Discovery in Life Science® ENZO LIFE SCIENCES, INC. Enzo Life Sciences, Inc., a subsidiary of Enzo Biochem, Inc., is organized to lead in the development, production, marketing, and sale of innovative life science research reagents worldwide. Now incorporating the skills, experience, and products of ALEXIS Biochemicals, acquired in 2007, BIOMOL International, acquired in 2008, and ASSAY DESIGNS, acquired in 2009, Enzo Life Sciences provides more than 25 years of business experience in the supply of research biochemicals, assay systems and biological reagents “Enabling Discovery in Life Science®.” Based on a very substantial intellectual property portfolio, Enzo Life Sciences, Inc. is a major developer and provider of advanced assay technologies across research and diagnostic markets. A strong portfolio of labeling probes and dyes provides life science environments with tools for target identification and validation, and high content analysis via gene expression analysis, nucleic acid detection, protein biochemistry and detection, molecular biology, and cellular analysis. • Genomic Analysis • Cellular Analysis • Post-translational Modification • Signal Transduction • Cancer & Immunology • Drug Discovery In addition to our wide range of catalog products, a complementary range of highly specialized custom services are also offered to provide tailor-made solutions for researchers. These include small molecule organic synthesis, peptide synthesis, protein expression, antibody production and immunoassay development. Enzo Life Sciences is proud to support responsibly- managed forests. This catalog was printed by an FSC (Forest Stewardship Council) certified printer on paper manufactured using responsibly-managed forests.