Receptor-specific Ubiquitination of β-Arrestin Directs Assembly and Targeting of Seven-transmembrane Receptor Signalosomes
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TLDR
Shenoy et al. as discussed by the authors showed that lysines at positions 11 and 12 in β-arrestin2 are specific and required sites for its AngII-mediated sustained ubiquitination.About:
This article is published in Journal of Biological Chemistry.The article was published on 2005-04-15 and is currently open access. It has received 166 citations till now. The article focuses on the topics: Endosome & Signal transducing adaptor protein.read more
Citations
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Journal ArticleDOI
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.
Journal ArticleDOI
Communicating with Hedgehogs.
Joan E. Hooper,Matthew P. Scott +1 more
TL;DR: Signalling by secreted Hedgehog (Hh) proteins is important for the development of many tissues and organs and the cellular machinery that is responsible for the unique molecular mechanisms of Hh signal transduction has been largely conserved during metazoan evolution.
Journal ArticleDOI
β-Arrestin-dependent, G Protein-independent ERK1/2 Activation by the β2 Adrenergic Receptor
Sudha K. Shenoy,Matthew T. Drake,Christopher D. Nelson,Daniel A. Houtz,Kunhong Xiao,Srinivasan Madabushi,Eric Reiter,Eric Reiter,Richard T. Premont,Olivier Lichtarge,Robert J. Lefkowitz +10 more
TL;DR: It is demonstrated that the β2AR can signal to ERK via a GRK5/6-β-arrestin-dependent pathway, which is independent of G protein coupling, and GRK2, membrane translocation of which requires Gβγ release upon G protein activation, was ineffective unless it was constitutively targeted to the plasma membrane by a prenylation signal.
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Regulation of Receptor Trafficking by GRKs and Arrestins
TL;DR: This chapter discusses the mechanisms that regulate receptor endocytic trafficking, emphasizing the role of GPCR kinases (GRKs) and arrestins in this process.
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.
References
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Journal ArticleDOI
The Ubiquitin System
Avram Hershko,Aaron Ciechanover +1 more
TL;DR: This review discusses recent information on functions and mechanisms of the ubiquitin system and focuses on what the authors know, and would like to know, about the mode of action of ubi...
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Erk and p38 mapk-activated protein kinases: a family of protein kinases with diverse biological functions
Philippe P. Roux,John Blenis +1 more
TL;DR: The identities of the MK substrates indicate that they play important roles in diverse biological processes, including mRNA translation, cell proliferation and survival, and the nuclear genomic response to mitogens and cellular stresses.
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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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cPLA2 is phosphorylated and activated by MAP kinase.
TL;DR: Treatment of cells with agents that stimulate the release of arachidonic acid causes increased serine phosphorylation and activation of cytosolic phospholipase A2 (cPLA2).
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Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes.
Louis M. Luttrell,Stephen S. G. Ferguson,Yehia Daaka,William E. Miller,Stuart Maudsley,G. J. Della Rocca,Fang-Tsyr Lin,H. Kawakatsu,K. Owada,D. K. Luttrell,Marc G. Caron,Robert J. Lefkowitz +11 more
TL;DR: Data suggest that beta-arrestin binding, which terminates receptor-G protein coupling, also initiates a second wave of signal transduction in which the "desensitized" receptor functions as a critical structural component of a mitogenic signaling complex.