Ubiquitination of β-Arrestin Links Seven-transmembrane Receptor Endocytosis and ERK Activation
Sudha K. Shenoy,Larry S. Barak,Kunhong Xiao,Seungkirl Ahn,Magali Berthouze,Arun K. Shukla,Louis M. Luttrell,Louis M. Luttrell,Robert J. Lefkowitz,Robert J. Lefkowitz +9 more
TLDR
Although β-arrestin ubiquitination is dispensable for β-Arrestin cytosol to membrane translocation and its “constitutive” interactions with some cytosolic proteins, it nevertheless is a prerequisite both for the formation of tight complexes with 7TMRs in vivo and for membrane compartment interactions that are crucial for downstream endocytic and signaling processes.About:
This article is published in Journal of Biological Chemistry.The article was published on 2007-10-05 and is currently open access. It has received 124 citations till now. The article focuses on the topics: Ubiquitin-conjugating enzyme & Endosome.read more
Citations
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Journal ArticleDOI
β-arrestin-mediated receptor trafficking and signal transduction
TL;DR: The traditional and novel functions of β-arrestins are assessed and the molecular attributes that might facilitate multiple interactions in regulating cell signaling and receptor trafficking are discussed.
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Therapeutic potential of β-arrestin- and G protein-biased agonists
TL;DR: The diversity of G protein- and β-arrestin-mediated functions and the therapeutic potential of selective targeting of these in disease states are highlighted.
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Beyond Desensitization: Physiological Relevance of Arrestin-Dependent Signaling
TL;DR: The role of arrestin-dependent heptahelical G protein-coupled receptors in the human genome has been investigated in this article. But, the role of the arrestin binding is not yet fully understood.
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Endosomes: A legitimate platform for the signaling train
TL;DR: Selective disruption of receptor signaling in endosomes, which can be accomplished by targeting endosomal-specific signaling pathways or by selective delivery of drugs to the endosome network, may provide novel therapies for disease.
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The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling.
TL;DR: The structure–function relationships that enable arrestins to perform their diverse roles are examined, addressing arrestin structure at the molecular level, the relationship between arrestin conformation and function, and sites of interaction between arrestins, GPCRs, and nonreceptor-binding partners.
References
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TAK1 is a ubiquitin-dependent kinase of MKK and IKK
TL;DR: The purification and identification of TRIKA2, which is composed of TAK1, TAB1 and TAB2, a protein kinase complex previously implicated in IKK activation through an unknown mechanism, indicate that ubiquitination has an important regulatory role in stress response pathways, including those of IKK and JNK.
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Transduction of receptor signals by beta-arrestins.
TL;DR: Another previously unappreciated strategy used by the receptors to regulate intracellular signaling pathways is indicated, which regulates aspects of cell motility, chemotaxis, apoptosis, and likely other cellular functions through a rapidly expanding list of signaling pathways.
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The ubiquitin system for protein degradation
Avram Hershko,Aaron Ciechanover +1 more
TL;DR: The Ubiquitin-C-TERMINAL HYDROLASES study highlights the importance of knowing the carrier and removal status of these components in the preparation of the UBIQUITIN-MEDIATED DEGRADATION.
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Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor.
Oscar B. Goodman,Jason G. Krupnick,Francesca Santini,Vsevolod V. Gurevich,Vsevolod V. Gurevich,Raymond B. Penn,Alison W. Gagnon,James H. Keen,Jeffrey L. Benovic +8 more
TL;DR: The results show that β-arrestin functions as an adaptor in the receptor-mediated endocytosis pathway, and suggest a general mechanism for regulating the trafficking of G-protein-coupled receptors.
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β-Arrestins and Cell Signaling
TL;DR: The signaling capacities of these versatile adapter molecules are reviewed and the possible implications for cellular processes such as chemotaxis and apoptosis are discussed.