Linked Life Data

17084806

Source:http://linkedlifedata.com/resource/pubmed/id/17084806

Statements in which the resource exists.
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pubmed-article:17084806pubmed:abstractTextG protein-coupled receptor kinases (GRKs) and arrestins are key participants in the canonical pathways leading to phosphorylation-dependent GPCR desensitization, endocytosis, intracellular trafficking and resensitization as well as in the modulation of important intracellular signaling cascades by GPCR. Novel studies have revealed a phosphorylation-independent desensitization mechanism operating through their RGS-homology (RH) domain and the recent determination of the crystal structures of GRK2 and GRK6 has uncovered interesting details on the structure-function relationships of these kinases. Emerging evidence indicates that the activity of GRKs is tightly modulated by mechanisms including phosphorylation by different kinases and interaction with several cellular proteins such as calmodulin, caveolin or RKIP. In addition, GRKs are involved in multiple interactions with non-receptor proteins (PI3K, Akt, GIT or MEK) that point to novel GRK cellular roles. In this article, our purpose is to describe the ever increasing map of functional interactions for GRK proteins as a basis to better understand its contribution to cellular processes.lld:pubmed
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pubmed-article:17084806pubmed:dateRevised2007-11-15lld:pubmed
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pubmed-article:17084806pubmed:articleTitleThe G protein-coupled receptor kinase (GRK) interactome: role of GRKs in GPCR regulation and signaling.lld:pubmed
pubmed-article:17084806pubmed:affiliationDepartamento de Biología Molecular and Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas-Universidad Autonoma de Madrid, Madrid, Spain.lld:pubmed
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