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Título

Activation of Ras and Rho GTPases and MAP Kinases by G-Protein-Coupled Receptors

AutorChiariello, Mario; Vaqué, José P.; Crespo, Piero ; Gutkind, J. Silvio
Palabras claveKinase assays
Western blot
Phosphorylation
Synthetic ligands
RASSLs
ERKs
GTP
Ras
Fecha de publicación2010
EditorSpringer
CitaciónMAP Kinase Signaling Protocols: 137-150 (2010)
SerieMethods in Molecular Biology
661
ResumenA complex intracellular signaling network mediates the multiple biological activities of G-protein-coupled receptors (GPCRs). Among them, monomeric GTPases and a family of closely related proline-targeted serine–threonine kinases, collectively known as Mitogen-Activated Protein Kinases (MAPKs), appears to play central roles in orchestrating the proliferative responses to multiple mitogens that act on GPCRs. Upon GDP/GTP exchange, monomeric GTPases control the phosphorylation of conserved threonine and tyrosine residues in MAPKs by their immediate upstream kinases, increasing their enzymatic activity and inducing their translocation to the nucleus where they phosphorylate transcription factors, thereby regulating the expression of genes playing a key role in normal and aberrant cell growth. Recently, a number of GPCRs have been engineered to provide exclusive activation by synthetic drug-like compounds while becoming insensitive to endogenous ligands. These engineered receptors, named Receptors Activated Solely by Synthetic Ligands (RASSLs), promise better understanding of GPCRs signaling in vitro and in vivo, thus representing ideal tools to selectively modulate MAPK signaling routes controlling a wide range of biological functions, from proliferation to differentiation, migration, invasion, and cell survival or death by apoptosis.
Descripción14 páginas, 2 figuras.
Versión del editorhttp://dx.doi.org/10.1007/978-1-60761-795-2_8
URIhttp://hdl.handle.net/10261/40502
DOI10.1007/978-1-60761-795-2_8
ISBN978-1-60761-794-5
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