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
Src-dependent Tyrosine Phosphorylation Regulates Dynamin Self-assembly and Ligand-induced Endocytosis of the Epidermal Growth Factor Receptor
Seungkirl Ahn,Jihee Kim,Carmen Lucaveche,Mary C. Reedy,Louis M. Luttrell,Robert J. Lefkowitz,Robert J. Lefkowitz,Yehia Daaka +7 more
TL;DR: It is demonstrated that phosphorylation of dynamin I by c-Src induces its self-assembly and increases its GTPase activity, and electron microscopic analyses reveal that tyrosine-phosphorylated Dynamin I spontaneously self-assembles into large stacks of rings.
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Beta-agonist- and prostaglandin E1-induced translocation of the beta-adrenergic receptor kinase: evidence that the kinase may act on multiple adenylate cyclase-coupled receptors.
TL;DR: The results suggest that the first step in homologous desensitization of the beta-adrenergic receptor may be an agonist-promoted translocation of beta-ar kinase from cytosol to plasma membrane and that beta-AR kinase may represent a more general adenylate cyclase-coupled receptor kinase that participates in regulating the function of many such receptors.
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G Protein-coupled Receptor Kinase 6A Phosphorylates the Na+/H+ Exchanger Regulatory Factor via a PDZ Domain-mediated Interaction
Randy A. Hall,Robert F. Spurney,Richard T. Premont,Nadeem Rahman,Jeremy T. Blitzer,Julie A. Pitcher,Robert J. Lefkowitz +6 more
TL;DR: It is shown that the primary site of constitutive NHERF phosphorylated in human embryonic kidney 293 (HEK-293) cells is Ser289, and that the stoichiometry of phosphorylation is near 1 mol/mol, which indicates that the endogenous “NHERF kinase” activity in HEk-293 cell lysates is sensitive to treatments that alter the activity of GRK6A.
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Identification of a Motif in the Carboxyl Terminus of β-Arrestin2 Responsible for Activation of JNK3
William E. Miller,Patricia McDonald,Sheng F. Cai,Michael Field,Roger J. Davis,Robert J. Lefkowitz +5 more
TL;DR: A mechanism by which β-arrestin2 functions as a scaffold protein in the JNK3 signaling pathway is delineated and the conserved docking site in β-Arrestin1 is implicate as an important factor in binding J NK3 and stimulating the phosphorylation of JNK 3 by MKK4.
Journal Article
The alpha 1C-adrenergic receptor: characterization of signal transduction pathways and mammalian tissue heterogeneity.
Debra A. Schwinn,Stella O. Page,John P. Middleton,Wulfing Lorenz,Stephen B. Liggett,Kyohei Yamamoto,Eduardo G. Lapetina,Marc G. Caron,Robert J. Lefkowitz,Susanna Cotecchia +9 more
TL;DR: The results indicate that the cloning and expression of differentalpha 1AR subtypes represents a valuable tool to elucidate functional correlates of alpha 1AR heterogeneity, and striking mammalian species heterogeneity.