Characterization of the Sites of Interactions that Mediate Binding of [beta]-arrestins to Lim Kinase and Cofilin Upon Par-2 Activation PDF Download
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Author: Rashid Awan
Publisher:
ISBN:
Category : Arrestins
Languages : en
Pages : 26
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Book Description
![Characterization of the Sites of Interactions that Mediate Binding of [beta]-arrestins to Lim Kinase and Cofilin Upon Par-2 Activation PDF](https://books.google.com/books/content/images/frontcover/-6OktgEACAAJ?fife=w80-h100)
Author: Rashid Awan
Publisher:
ISBN:
Category : Arrestins
Languages : en
Pages : 26
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Author: Alice Lin
Publisher:
ISBN:
Category : Arrestins
Languages : en
Pages : 105
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Book Description
Author: Puneet Kumar
Publisher:
ISBN:
Category : Cellular signal transduction
Languages : en
Pages : 282
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Author: Jungah Min
Publisher:
ISBN:
Category : G proteins
Languages : en
Pages : 116
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Book Description
[Beta]-arrestins, originally discovered in the context of G protein-coupled receptor (GPCR) desensitization and internalization, also function in signaling of these receptors independently of G protein coupling. These novel functions involve the role for [Beta]-arrestins as scaffolds. It has been reported that [Beta]-arrestins interact with a number of binding partners including trafficking proteins, cytosolic kinases, cytoskeletal proteins, and non-receptor tyrosine kinase. Downstream of protease-activated receptor-2 (PAR-2), [Beta]-arrestin scaffolds the components of the ERK cascade, c-Raf, MEK1, and ERK1/2 with the receptor at the plasma membrane, leading to activation of cytoplasmic/membrane ERK1/2 signaling independently of G-protein coupling. Furthermore, we previously reported that stimulation of PAR-2 induced prolonged activation of ERK1/2 in pseudopodia in a [Beta]-arrestin-dependent manner and [Beta]-arrestins were required in PAR-2-mediated ERK1/2 activation at the membrane and cell migration in metastatic tumor cell lines, suggesting [Beta]-arrestin-dependent ERK1/2 activation might play a role in cell motility. Although a number of recent studies reported that [Beta]-arrestins are required for ERK1/2 activation independently of G protein coupling, molecular mechanism of [Beta]-arrestin- mediated ERK1/2 activation via c-Raf has remained unclear. We hypothesized that the ability of [Beta]-arrestins to scaffold and prolong MAPK signaling at the membrane, is dependent upon precise molecular interactions that are facilitated by interaction of [Beta]-arrestins with PAR-2. To investigate the hypothesis, we determine the sites/domains in [Beta]-arrestin-1 that interact with components of the ERK module (c-Raf, MEK1, and ERK1/2) both in vitro and in cells using GST pull down assay, sandwich immunoassay, and co-immunoprecipitation and investigate the role of these identified regions of [Beta]-arrestin for interaction and activation of ERK1/2 using truncated mutants of [Beta]-arrestin or [Beta]-arrestin mutants lacking domains. In addition, a mysterious link in functional mechanism of [Beta]-arrestin-mediated ERK1/2 activation is how c-Raf relieves autoinhibition engendering a conformation change from a closed, inactive state to an open, active state, without small GTPase Ras, which was known to be critical for c-Raf activation in the classical G protein-dependent ERK activation. We hypothesized that [Beta]-arrestins behave similar to Ras for [Beta]-arrestin-dependent ERK activation to relieve autoinhibition of c-Raf. We show that [Beta]-arrestin-1 binds to the regulatory domain of c-Raf where Ras was indentified to bind. Therefore, binding of [Beta]-arrestin-1 to c-Raf might ensure formation of scaffolding complex containing [Beta]-arrestin-1 and the ERK cascade and play a critical role to activate c-Raf in [Beta]-arrestin-dependent ERK1/2 activation.
Author: Marc Thiriet
Publisher: Springer Science & Business Media
ISBN: 1461443695
Category : Science
Languages : en
Pages : 1073
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Book Description
The volumes in this authoritative series present a multidisciplinary approach to modeling and simulation of flows in the cardiovascular and ventilatory systems, especially multiscale modeling and coupled simulations. The cardiovascular and respiratory systems are tightly coupled, as their primary function is to supply oxygen to and remove carbon dioxide from the body's cells. Because physiological conduits have deformable and reactive walls, macroscopic flow behavior and prediction must be coupled to phenomenological models of nano- and microscopic events in a corrector scheme of regulated mechanisms when the vessel lumen caliber varies markedly. Therefore, investigation of flows of blood and air in physiological conduits requires an understanding of the biology, chemistry, and physics of these systems together with the mathematical tools to describe their functioning. Volume 4 is devoted to major sets of intracellular mediators that transmit signals upon stimulation of cell-surface receptors. Activation of signaling effectors triggers the release of substances stored in cellular organelles and/or gene transcription and protein synthesis. Complex stages of cell signaling can be studied using proper mathematical models, once the role of each component is carefully handled. Volume 4 also reviews various categories of cytosolic and/or nuclear mediators and illustrates some major signal transduction pathways, such as NFkappaB axis, oxygen sensing, and mechanotransduction.
Author: Ralph A. Bradshaw
Publisher: Academic Press
ISBN: 0080920918
Category : Science
Languages : en
Pages : 3188
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Book Description
Handbook of Cell Signaling, Three-Volume Set, 2e, is a comprehensive work covering all aspects of intracellular signal processing, including extra/intracellular membrane receptors, signal transduction, gene expression/translation, and cellular/organotypic signal responses. The second edition is an up-to-date, expanded reference with each section edited by a recognized expert in the field. Tabular and well illustrated, the Handbook will serve as an in-depth reference for this complex and evolving field. Handbook of Cell Signaling, 2/e will appeal to a broad, cross-disciplinary audience interested in the structure, biochemistry, molecular biology and pathology of cellular effectors. - Contains over 350 chapters of comprehensive coverage on cell signaling - Includes discussion on topics from ligand/receptor interactions to organ/organism responses - Provides user-friendly, well-illustrated, reputable content by experts in the field
Author: Kermit L. Carraway
Publisher: Springer Science & Business Media
ISBN: 3662129930
Category : Science
Languages : en
Pages : 293
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Book Description
This monograph explores the relationships between cell signaling and the cytoplasmic cytoskeleton in fundamental cell processes, thus bridging the gap between two very active aspects of molecular cell biology. It covers the two main - and reciprocal - questions of these relationships: How are structure and function of the cytoskeleton affected by external signals which impinge on the cell? How does the cytoskeleton influence the cellular signaling processes which determine cell behavior?
Author: Angel L. Pey
Publisher: Academic Press
ISBN: 0128191333
Category : Science
Languages : en
Pages : 452
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Book Description
Protein Homeostasis Diseases: Mechanisms and Novel Therapies offers an interdisciplinary examination of the fundamental aspects, biochemistry and molecular biology of protein homeostasis disease, including the use of natural and pharmacological small molecules to treat common and rare protein homeostasis disorders. Contributions from international experts discuss the biochemical and genetic components of protein homeostasis disorders, the mechanisms by which genetic variants may cause loss-of-function and gain-of-toxic-function, and how natural ligands can restore protein function and homeostasis in genetic diseases. Applied chapters provide guidance on employing high throughput sequencing and screening methodologies to develop pharmacological chaperones and repurpose approved drugs to treat protein homeostasis disorders. - Provides an interdisciplinary examination of protein homeostasis disorders, with an emphasis on treatment strategies employing small natural and pharmacological ligands - Offers applied approaches in employing high throughput sequencing and screening to develop pharmacological chaperones to treat protein homeostasis disease - Gathers expertise from a range of international chapter authors who work across various biological methods and disease specific disciplines of relevance
Author: Tamas Balla
Publisher: Springer Science & Business Media
ISBN: 9400730152
Category : Medical
Languages : en
Pages : 467
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Book Description
Phosphoinositides play a major role in cellular signaling and membrane organization. During the last three decades we have learned that enzymes turning over phosphoinositides control vital physiological processes and are involved in the initiation and progression of cancer, inflammation, neurodegenerative, cardiovascular, metabolic disease and more. In two volumes, this book elucidates the crucial mechanisms that control the dynamics of phosphoinositide conversion. Starting out from phosphatidylinositol, a chain of lipid kinases collaborates to generate the oncogenic lipid phosphatidylinositol(3,4,5)-trisphosphate. For every phosphate group added, there are specific lipid kinases – and phosphatases to remove it. Additionally, phospholipases can cleave off the inositol head group and generate poly-phosphoinositols, which act as soluble signals in the cytosol. Volume II extends into the role of phosphoinositides in membrane organization and vesicular traffic. Endocytosis and exocytosis are modulated by phosphoinositides, which determine the fate and activity of integral membrane proteins. Phosphatidylinositol(4,5)-bisphosphate is a prominent flag in the plasma membrane, while phosphatidylinositol-3-phosphate decorates early endosomes. The Golgi apparatus is rich in phosphatidylinositol-4-phosphate, stressed cells increase phosphatidylinositol(3,5)-bisphosphate, and the nucleus has a phosphoinositide metabolism of its own. Phosphoinositide-dependent signaling cascades and the spatial organization of distinct phosphoinositide species are required in organelle function, fission and fusion, membrane channel regulation, cytoskeletal rearrangements, adhesion processes, and thus orchestrate complex cellular responses including growth, proliferation, differentiation, cell motility, and cell polarization.
Author: Vsevolod V. Gurevich
Publisher: Springer
ISBN: 9783319861913
Category : Science
Languages : en
Pages : 0
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Book Description
This volume summarizes our current understanding of the structural basis of the functions of arrestin family of proteins. Arrestins were first discovered as key players in the desensitization of G protein-coupled receptors (GPCRs). Recent studies showed that arrestins are important signal transducers in their own right, organizing multi-protein complexes and scaffolding numerous signaling cascades that regulate cell proliferation, differentiation, and apoptotic death. Here arrestin functions are described primarily from the structural prospective. The book covers basal structure of arrestin proteins, receptor binding-induced conformational changes in arrestins, as well as the structure of “pre-activated” mutants. Particular focus is on the arrestin elements interacting with numerous binding partners, GPCRs and cytoplasmic signaling proteins. We expect that this information and insights will help to understand and exploit the phenomenon of signaling bias, which is a new promising direction in drug discovery. The chapters are written by the world-class specialists in the field, mostly the people who actually contributed the data discussed. The book gives coherent historical prospective and describes the most recent findings. The book would be particularly useful for scientists in academia and industry working in the fields of pharmacology, cell biology, structural biology, and drug discovery. We expect that the focus on the molecular basis of protein-protein interactions would help to develop novel tools for engaging this important type of targets for research and therapeutic purposes.
