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  • 1
    Keywords: Medicine ; Gene Therapy ; Toxicology ; Biochemistry ; Cell receptors ; Cytology ; Biomedicine ; Pharmacology/Toxicology ; Biochemistry, general ; Protein Structure ; Gene Therapy ; Cell Physiology ; Receptors ; Springer eBooks
    Description / Table of Contents: Therapeutic Potential of Small Molecules and Engineered Proteins.-Arrestin Interactions with G Protein-coupled Receptors -- Arrestin-biased GPCR℗ Agonists -- Arrestin-1 Expression Levels, Rod Function and Health -- Protective Functions of Arrestin-1 in Photoreceptors -- Arrestin-4 and Cone Function -- Enhanced Phosphorylation-independent Arrestins and Gene Therapy -- Targeting Particular Receptors with Redesigned Non-visual Arrestins.-℗ Arrestins binding to clathrin, AP2 and Role in GPCR trafficking -- Arrestins in Ubiquitination and Deubiquitination -- Arrestin Self-association -- Arrestin-dependent Activation of ERK and Src -- Arrestin-dependent Activation of JNK Family Kinases -- Arrestin-Mediated P38 Activation.-℗ Arrestin-dependent PDE Localization -- Arrestins in Cell Migration -- Arrestins in Host-pathogen Interactions -- Arrestin Regulation of Small GTPases -- GPCRs and Arrestins in Airways: Implications for Asthma -- Arrestins as Regulatory Signaling Hubs in Cancer Pathways -- Arrestins in Pain and Anesthesia
    Abstract: This volume describes our current understanding of the biological role of visual and non-visual arrestins in different cells and tissues, focusing on the mechanisms of arrestin-mediated regulation of GPCRs and non-receptor signaling proteins in health and disease. The book covers wide range of arrestin functions, emphasizing therapeutic potential of targeting arrestin interactions with individual partners
    Pages: VIII, 447 p. 53 illus., 42 illus. in color. : online resource.
    ISBN: 9783642411991
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  • 2
    Keywords: Medicine ; Pharmacology ; Biomedicine ; Pharmacology/Toxicology ; Springer eBooks
    Description / Table of Contents: G Protein-Coupled Receptor Kinases (GRKs) History: Evolution and Discovery -- Structure and Function of G Protein-Coupled Receptor Kinases 1 and 7 -- Visual G Protein-Coupled Receptor Kinases -- Molecular Basis for Targeting, Inhibition, and Receptor Phosphorylation in the G Protein-Coupled Receptor Kinase 4 Subfamily -- “Barcode” and Differential Effects of GPCR Phosphorylation by Different GRKs -- Cell-Type Specific GRK2 Interactomes: Physiopathological Implications -- Differential Regulation of IGF-1 and Insulin Signaling by GRKs -- Differential Control of Potassium Channel Activity by GRK2 -- Critical Role of GRK2 in the Prevention of Chronic Pain -- Roles of GRK Dysfunction in Alzheimer’s Pathogenesis -- Regulation of Dopamine-Dependent Behaviors by G Protein-Coupled Receptor Kinases -- G Protein-Coupled Receptors and Their Kinases in Cardiac Regulation -- GRK Roles in C. elegans -- Evolutionarily Conserved Role of G Protein-Coupled Receptor Kinases in the Hedgehog Signaling Pathway
    Abstract: This collection explores up-to-date descriptions of known G protein-coupled receptor kinase (GRK)-dependent mechanisms, both associated with G protein-coupled receptor (GPCR) functions and the receptor-independent. The chapters cover a wide range of studies from invertebrates to humans, with sections of the volume covering GRK structure, mechanisms of activation, and interaction with GPCRs, GRKs in cell signaling, as well as physiological and pathophysiological mechanisms regulated by GRKs. Written for the Methods in Pharmacology and Toxicology series, this book features the kind of practical detail necessary for success in the laboratory. Authoritative and timely, G Protein-Coupled Receptor Kinases features the kind of comprehensive mechanistic elucidation of GRK functions and their regulation in cells necessary for a better understanding of cell biology as well as for devising novel research approaches and therapeutic strategies
    Pages: XI, 329 p. 36 illus., 33 illus. in color. : online resource.
    ISBN: 9781493937981
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  • 3
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    Cham : Springer International Publishing
    Keywords: Life sciences ; Biochemistry ; Proteins ; Life sciences ; Animal Biochemistry ; Protein Science ; Protein Structure ; Springer eBooks
    Description / Table of Contents: Arrestins: discovery of the family and functional role of conformational flexibility -- Overview of arrestin-mediated signaling with receptors and non-receptor binding partners -- Initial crystallographic studies of visual arrestin: insights and perspectives -- Structural basis for b-arrestins in GPCR trafficking -- Arrestin-3: the structural basis of lower receptor selectivity -- Phosphate sensor and construction of phosphorylation-independent arrestins -- Comprehensive analysis of the role of arrestin residues in receptor binding -- How arrestin recognizes and binds active GPCRs -- Localization of conformational dynamics of arrestins by HDX-MS -- GPCR footprint on arrestins and manipulation of receptor specificity -- The structure of the polar core mutant R175E and its functional implications -- Active conformations of arrestins: expected and unexpected changes -- The arrestin-receptor complex: exciting answers and new questions -- Scaffolding c-Jun N-terminal kinase cascades: mechanistic insights from the reconstituted arrestin-JNK cascades -- Arrestin-dependent ERK activation and its disruption -- The functional role of the conformational changes in arrestin upon activation -- Is signaling specificity encoded in arrestin conformation? -- Monofunctional elements of multi-functional arrestin proteins -- Arrestins in cell death
    Abstract: 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
    Pages: IX, 304 p. 53 illus., 51 illus. in color. : online resource.
    ISBN: 9783319575537
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  • 4
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] As internalization of P2AR appears to occur through clathrin-coated pits7, we considered that arrestins might function to target P2AR to clathrin-coated pits. To test this, we examined whether arrestins interact with clathrin, the major structural protein of coated pits. In vitro translated ...
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] β-Adrenergic receptor (βAR) stimulation increases cytosolic Ca2+ to physiologically augment cardiac contraction, whereas excessive βAR activation causes adverse cardiac remodeling, including myocardial hypertrophy, dilation and dysfunction, in individuals with myocardial infarction. ...
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The binding of arrestin to rhodopsin is initiated by the interaction of arrestin with the phosphorylated rhodopsin C-terminus and/or the cytoplasmic loops, followed by conformational changes that expose an additional high-affinity site on arrestin. Here we use an arrestin mutant (R175E) that binds similarly to phosphorylated and unphosphorylated, wild-type rhodopsin to identify rhodopsin elements other than C-terminus important for arrestin interaction. R175E-arrestin demonstrated greatly reduced binding to unphosphorylated cytoplasmic loop mutants L72A, N73A, P142A and M143A, suggesting that these residues are crucial for high-affinity binding. Interestingly, when these rhodopsin mutants are phosphorylated, R175E-arrestin binding is less severely affected. This effect of phosphorylation on R175E-arrestin binding highlights the co-operative nature of the multi-site interaction between arrestin and the cytoplasmic loops and C-terminus of rhodopsin. However, a combination of any two mutations disrupts the ability of phosphorylation to enhance binding of R175E-arrestin. N73A, P142A and M143A exhibited accelerated rates of dissociation from wild-type arrestin. Using sensitivity to calpain II as an assay, these cytoplasmic loop mutants also demonstrated reduced ability to induce conformational changes in arrestin that correlated with their reduced ability to bind arrestin. These results suggest that arrestin bound to rhodopsin is in a distinct conformation that is co-ordinately regulated by association with the cytoplasmic loops and the C-terminus of rhodopsin.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Arrestins and G protein-coupled receptor kinases (GRKs) are key players in homologous desensitization of G protein-coupled receptors. Two non-visual arrestins, arrestin2 and 3, and five GRKs (GRK2, 3, 4, 5 and 6) are involved in desensitization of many receptors. Here, we demonstrate a steady increase in arrestin2 expression during prenatal development. The density of arrestin2 mRNA is higher in differentiated areas as compared with proliferative zones, whereas arrestin3 mRNA shows the opposite distribution. At embryonic day 14, concentrations of arrestin proteins are similar (32–34 nm). Later in development, arrestin2 expression rises, leading to a fourfold excess of arrestin2 over arrestin3 at birth (48 vs. 11 ng/mg protein or 102 vs. 25 nm). Among GRKs, only GRK5 increased with embryonic age from 124 nm at E14 to 359 nm at birth. Similarly, in vitro differentiation of cultured precursor cells, neurospheres, leads to a significant up-regulation of arrestin2 resulting in 〉 20-fold excess of arrestin2 (160 vs. 7 nm). GRK5 is the only subtype increased with neurosphere differentiation, although the change is only about twofold. The data demonstrate selective increases in the expression of arrestin2 associated with neural development and suggest specific yet unappreciated roles for arrestin2 in neural differentiation.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Dopamine D1 receptor interactions with arrestins have been characterized using heterologously expressed D1 receptor and arrestins. The purpose of this study was to investigate the interaction of the endogenous D1 receptor with endogenous arrestin2 and 3 in neostriatal neurons. Endogenous arrestin2 and 3 in striatal homogenates bound to the C-terminus of the D1 receptor in a glutathione-S-transferase (GST) pulldown assay, with arrestin3 binding more strongly. The D1 C-terminus and, to a lesser extent, the third cytoplasmic loop also bound purified arrestin2 and 3. In neostriatal neurons, 2, 5, and 20 min agonist treatment increased the colocalization of the D1 receptor and arrestin3 immunoreactivity without altering the colocalization of the D1 receptor and arrestin2. Further, agonist treatment for 5 and 20 min caused translocation of arrestin3, but not arrestin2, to the membrane. The binding of arrestin3, but not arrestin2, to the D1 receptor was increased as assessed by coimmunoprecipitation after agonist treatment for 5 and 20 min. Agonist treatment of neurons induced D1 receptor internalization (35–45%) that was maximal within 2–5 min, a time-course similar to that of the increase in colocalization of the D1 receptor with arrestin3. These data indicate that the D1 receptor preferentially interacts with arrestin3 in neostriatal neurons.
    Type of Medium: Electronic Resource
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