R
Robert J. Lefkowitz
Researcher at Howard Hughes Medical Institute
Publications - 867
Citations - 153371
Robert J. Lefkowitz is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Receptor & G protein-coupled receptor. The author has an hindex of 214, co-authored 860 publications receiving 147995 citations. Previous affiliations of Robert J. Lefkowitz include University of Nice Sophia Antipolis & University of Stuttgart.
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Journal ArticleDOI
Ras-dependent Mitogen-activated Protein Kinase Activation by G Protein-coupled Receptors CONVERGENCE OF Gi- AND Gq-MEDIATED PATHWAYS ON CALCIUM/CALMODULIN, Pyk2, AND Src KINASE
Gregory J. Della Rocca,Tim van Biesen,Yehia Daaka,Deirdre K. Luttrell,Louis M. Luttrell,Robert J. Lefkowitz +5 more
TL;DR: Results indicate that calcium-calmodulin plays a central role in the calcium-dependent regulation of tyrosine phosphorylation by G protein-coupled receptors in some systems, and indicate that in HEK-293 cells, the Gβγ subunit-mediated α2A-AR- and the Gαq/11-mediated βARK1ct-mediated Erk1/2 activation pathways converge at the level of phospholipase C.
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Dual modulation of cell survival and cell death by beta(2)-adrenergic signaling in adult mouse cardiac myocytes.
TL;DR: In this article, the authors investigate the role of β-adrenergic receptor (AR) and β-AR subtypes in regulating cardiomyocyte survival and apoptosis and explore underlying mechanisms.
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Distinct β-arrestin- and G protein-dependent pathways for parathyroid hormone receptor-stimulated ERK1/2 activation
Diane Gesty-Palmer,Minyong Chen,Eric Reiter,Seungkirl Ahn,Christopher D. Nelson,Shuntai Wang,Allen E. Eckhardt,Conrad L. Cowan,Robert F. Spurney,Louis M. Luttrell,Louis M. Luttrell,Robert J. Lefkowitz +11 more
TL;DR: It is concluded that PTH stimulates ERK1/2 through several distinct signal transduction pathways: an early G protein-dependent pathway meditated by PKA and PKC and a late pathway independent of G proteins mediated through β-arrestins.
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The binding site for the beta gamma subunits of heterotrimeric G proteins on the beta-adrenergic receptor kinase.
TL;DR: Three distinct approaches are employed to identify the region within the carboxyl terminus of beta ARK which binds beta gamma and thereby results in membrane translocation, and provide important tools for the study of G protein-coupled receptor desensitization, as well as for the investigation of beta gamma activation of other Gprotein-effector systems.
Journal ArticleDOI
Regulation of G Protein-Coupled Receptor Kinases and Arrestins During Receptor Desensitization
TL;DR: With at least 1000 family members encoded by mammalian genomes, the G protein-coupled receptors represent the most diverse group of signaling proteins known.