The Hsp70 Molecular Chaperone Machines

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The Hsp70 Molecular Chaperone Machines
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Author : Matthias P. Mayer
language : en
Publisher: Frontiers Media SA
Release Date : 2017-03-24
The Hsp70 Molecular Chaperone Machines written by Matthias P. Mayer and has been published by Frontiers Media SA this book supported file pdf, txt, epub, kindle and other format this book has been release on 2017-03-24 with categories.
Members of the HSP70 family form a central hub of the molecular chaperone network, controlling protein homeostasis in prokaryotes and in the ATP-containing compartments of the eukaryotic cells. The heat-inducible form HSPA1A (HSP70), its constitutive cytosolic cognate HSPA8 (Hsc70), its endoplasmic reticulum form HSPA5 (BiP), and its mitochondrial form HSPA9 (Mortalin), as well as the more distantly related HSPHs (HSP110s), make up 1-2 % of the total mass of proteins in human cells. They use the energy of ATP-hydrolysis to prevent and forcefully revert the process of protein misfolding and aggregation during and following various stresses, presumably by working as unfoldases to lift aberrant conformers out of kinetic traps. As such, HSP70s, in cooperation with their J-domain co-chaperones and nucleotide exchange factors (NEFs) and co-disaggregases, form an efficient network of cellular defenses against the accumulation of cytotoxic misfolded protein conformers, which may cause degenerative diseases such as Parkinson's and Alzheimer's disease, diabetes, and aging in general. In addition to their function in repair of stress-induced damage, HSP70s fulfill many housekeeping functions, including assisting the de novo folding and maturation of proteins, driving the translocation of protein precursors across narrow membrane pores into organelles, and by controlling the oligomeric state of key regulator protein complexes involved in signal transduction and vesicular trafficking. For reasons not well understood, HSP70s are also found on the surface of some animal cells, in particular cancer cells where they may serve as specific targets for cancer immunotherapy. Here, we gathered seven mini reviews, each presenting a complementary aspect of HSP70’s structure and function in bacteria and eukaryotes, under physiological and stressful conditions. These articles highlight how, the various members of this conserved family of molecular chaperones, assisted by their various J-domain and NEF cochaperones and co-disaggregases, harness ATP hydrolysis to perform a great diversity of life-sustaining cellular functions using a similar molecular mechanism.
Structure And Action Of Molecular Chaperones Machines That Assist Protein Folding In The Cell
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Author : Lila M Gierasch
language : en
Publisher: World Scientific
Release Date : 2016-08-08
Structure And Action Of Molecular Chaperones Machines That Assist Protein Folding In The Cell written by Lila M Gierasch and has been published by World Scientific this book supported file pdf, txt, epub, kindle and other format this book has been release on 2016-08-08 with Science categories.
This unique volume reviews the beautiful architectures and varying mechanical actions of the set of specialized cellular proteins called molecular chaperones, which provide essential kinetic assistance to processes of protein folding and unfolding in the cell. Ranging from multisubunit ring-shaped chaperonin and Hsp100 machines that use their central cavities to bind and compartmentalize action on proteins, to machines that use other topologies of recognition — binding cellular proteins in an archway or at the surface of a 'clamp' or at the surface of a globular assembly — the structures show us the ways and means the cell has devised to assist its major effectors, proteins, to reach and maintain their unique active forms, as well as, when required, to disrupt protein structure in order to remodel or degrade. Each type of chaperone is beautifully illustrated by X-ray and EM structure determinations at near- atomic level resolution and described by a leader in the study of the respective family. The beauty of what Mother Nature has devised to accomplish essential assisting actions for proteins in vivo is fully appreciable.
The Molecular Chaperones Interaction Networks In Protein Folding And Degradation
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Author : Walid A. Houry
language : en
Publisher: Springer
Release Date : 2014-09-01
The Molecular Chaperones Interaction Networks In Protein Folding And Degradation written by Walid A. Houry and has been published by Springer this book supported file pdf, txt, epub, kindle and other format this book has been release on 2014-09-01 with Science categories.
Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved in other cellular functions including protein translocation across membranes, vesicle fusion events, and protein secretion. In recent years, tremendous advances have been made in our understanding of the biology, biochemistry, and biophysics of function of molecular chaperones. In addition, recent technical developments in the fields of proteomics and genomics allowed us to obtain a global view of chaperone interaction networks. Finally, there is now a growing interest in the role of molecular chaperones in diseases. This book will provide a comprehensive analysis of the structure and function of the diverse systems of molecular chaperones and their role in cell stress responses and in diseases from a global network perspective.
Molecular Chaperones In Human Disorders
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Author :
language : en
Publisher: Academic Press
Release Date : 2019-01-09
Molecular Chaperones In Human Disorders written by and has been published by Academic Press this book supported file pdf, txt, epub, kindle and other format this book has been release on 2019-01-09 with Science categories.
Molecular Chaperones in Human Disorders, Volume 114 in the Advances in Protein Chemistry and Structural Biology series, provides an overview of current developments in mechanisms underlying DNA repair and their involvement in maintaining chromatin repair, the balance between chromosomal repair pathways, tumorigenesis, immune signaling and infection-induced inflammation. Chapters in this new release cover Functional principles and regulation of molecular chaperones, Chaperones and retinal disorders, Protein misfolding and degradation in genetic diseases, Chaperone dysfunction in hereditary myopathic diseases, Diseases caused by functional disorder of molecular chaperones residing in the endoplasmic reticulum, and many other timely topics. - Describes advances in our understanding on DNA repair mechanisms and the involvement of their dysregulation in promoting diseases - Provides an ideal resource for a very wide audience of specialists, researchers and students - Contains timely chapters written by well-renown authorities in their field - Presents information that is well supported by a number of high quality illustrations, figures and tables
Molecular Chaperones In The Cell
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Author : Peter A. Lund
language : en
Publisher:
Release Date : 2001
Molecular Chaperones In The Cell written by Peter A. Lund and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2001 with Science categories.
Interest in molecular chaperones has grown exponentially over the last decade. Molecular Chaperones recognise nascet and unfolded polypeptide chains and are often essential for their folding, proteolytic processing, intracellular targeting, and secretion. They are vital for cell growth, with key roles in processes as diverse as signal transduction and stress survival. Much work has already been done in understanding the structure and function of the major molecular chaperones, and more recently the emphasis in research has shifted towrd exploring their precise roles in many different processes with which they are involved inside the cell. This aspect of molecular chaperone biology is the focus of this book. Here, the field's leading experts synthesise our body of knowledge into succinct chapters, and the reader gains not only a fuller understanding of the roles of chaperones in the context of cellular processes, but also an insight into the nature of these proteins and their breath of definition. This book represents an invaluable summary of the state of research in this fast moving highly important branch of molecular biology, which has ramifications for understanding not only many diverse cellular processes, but also give important insights into diseases such as BSE, CJD, and Alzhemier's disease, which invole protein misfolding.
Molecular Chaperones In Health And Disease
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Author : Matthias Gaestel
language : en
Publisher: Springer Science & Business Media
Release Date : 2005-12-29
Molecular Chaperones In Health And Disease written by Matthias Gaestel and has been published by Springer Science & Business Media this book supported file pdf, txt, epub, kindle and other format this book has been release on 2005-12-29 with Science categories.
Molecular chaperones are involved in a wide variety of essential cellular processes in living cells. A subset of molecular chaperones have been initially described as heat shock proteins protecting cells from stress damage by keeping cellular proteins in a folding competent state and preventing them from irreversible aggregation. Later it became obvious that molecular chaperones are also expressed constitutively in the cell and are involved in complex processes such as protein synthesis, intracellular protein transport, post-translational modification and secretion of proteins as well as receptor signalling. Hence, it is not surprising that molecular chaperones are implicated in the pathogenesis of many relevant diseases and could be regarded as potential pharmacological targets. Starting with the analysis of the mode of action of chaperones at the molecular, cellular and organismic level, this book will then describe specific aspects where modulation of chaperone action could be of pharmacological and therapeutic interest.
The Networking Of Chaperones By Co Chaperones
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Author : Gregory Lloyd Blatch
language : en
Publisher: Springer
Release Date : 2014-12-08
The Networking Of Chaperones By Co Chaperones written by Gregory Lloyd Blatch and has been published by Springer this book supported file pdf, txt, epub, kindle and other format this book has been release on 2014-12-08 with Medical categories.
Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets. The book will be a resource for both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology.
Structural Organization Of The Hsp90 Hsp70 Based Chaperone Machinery And Its Interaction With The Glucocorticoid Receptor Ligand Binding Domain
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Author : Patrick J. M. Murphy
language : en
Publisher:
Release Date : 2003
Structural Organization Of The Hsp90 Hsp70 Based Chaperone Machinery And Its Interaction With The Glucocorticoid Receptor Ligand Binding Domain written by Patrick J. M. Murphy and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2003 with categories.
Molecular Chaperones And Folding Catalysts
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Author : Bernd Bakau
language : en
Publisher: CRC Press
Release Date : 2003-09-02
Molecular Chaperones And Folding Catalysts written by Bernd Bakau and has been published by CRC Press this book supported file pdf, txt, epub, kindle and other format this book has been release on 2003-09-02 with Science categories.
One of the most intriguing discoveries in molecular biology in the last decade is the existence of an evolutionary conserved and essential system, consisting of molecular chaperones and folding catalysts, which promotes the folding of the proteins in the cell. This text summarizes our current knowledge of the cellular roles, the regulation and the mechanism of action of this system. It has a broad scope, covering cell biological, genetic and biochemical aspects of protein folding in cells from bacteria to man. Particularly appropriate to researchers working in basic and applied aspects of molecular medicine, this volume should also prove useful as an up-to-date reference book and as a textbook for specialized university courses.
Molecular Chaperones And Neurodegeneration
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Author : Cintia Roodveldt
language : en
Publisher: Frontiers Media SA
Release Date : 2017-12-06
Molecular Chaperones And Neurodegeneration written by Cintia Roodveldt and has been published by Frontiers Media SA this book supported file pdf, txt, epub, kindle and other format this book has been release on 2017-12-06 with categories.
Molecular chaperones or heat-shock proteins (HSPs) play essential roles in safeguarding structural stability and preventing misfolding and aggregation of proteins, and maintaining the proteome functionality in the cell. For over two decades until the present time, new functions have been discovered and several molecular mechanisms have been elucidated for many chaperones, while the field is being continuously challenged by new open questions. Probably as a consequence of the increasing research on the molecular bases of neurodegenerative diseases, and the realisation that many such disorders are linked to protein misfolding processes, unleashing the roles and mechanisms of chaperones in the context of neurodegeneration has become a prime scientific goal. This e-book contains a diversity of reviews, perspective and original research articles highlighting the importance and potential of this emerging subject.