Regulation of transmembrane signaling by receptor phosphorylation.
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Summary
The role of phosphorylation in regulating receptor function dramatically extends the range of regulatory control of this important covalent modification.
- Type
- review
- Published
- 1987-03-27
- Cited by
- 584
- References
- 105
- OpenAlex
- https://openalex.org/W2001578819
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:25147672
Keywords
Biology, Enzyme-linked receptor, Cell biology, Interleukin-13 receptor, Phosphorylation
References
- Characterization of insulin-like growth factor I-stimulated tyrosine kinase activity associated with the beta-subunit of type I insulin-like growth factor receptors of rat liver cells.
- Antibodies to the autophosphorylation sites of the epidermal growth factor receptor protein‐tyrosine kinase as probes of structure and function.
- Regulation of adrenergic receptor function by phosphorylation. II. Effects of agonist occupancy on phosphorylation of alpha 1- and beta 2-adrenergic receptors by protein kinase C and the cyclic AMP-dependent protein kinase.
- Epidermal growth factor and potent phorbol tumor promoters induce epidermal growth factor receptor phosphorylation in a similar but distinctively different manner in human epidermoid carcinoma A431 cells.
- Identification of serine 24 as the unique site on the transferrin receptor phosphorylated by protein kinase C.
- Insulin stimulates cellular iron uptake and causes the redistribution of intracellular transferrin receptors to the plasma membrane.
- Differences in the sites of phosphorylation of the insulin receptor in vivo and in vitro.
- Autophosphorylation and protein kinase C phosphorylation of the epidermal growth factor receptor. Effect on tyrosine kinase activity and ligand binding affinity.
- Tumor-promoting phorbol diesters mediate phosphorylation of the epidermal growth factor receptor.
- Characterization of platelet-derived growth factor-stimulated phosphorylation in cell membranes.
- Inhibition of epidermal growth factor binding to mouse cultured cells by fibroblast-derived growth factor. Evidence for an indirect mechanism.
- Suppression of protein tyrosine kinase activity of the epidermal growth factor receptor by epidermal growth factor.
- beta-Adrenergic regulation of insulin and epidermal growth factor receptors in rat adipocytes.
- Tumor-promoting phorbol esters increase the Km of the ATP-binding site of the insulin receptor kinase from rat adipocytes.
- Desensitization of turkey erythrocyte adenylate cyclase. Beta-adrenergic receptor phosphorylation is correlated with attenuation of adenylate cyclase activity.
- Mechanism of phorbol diester-induced regulation of surface transferrin receptor involves the action of activated protein kinase C and an intact cytoskeleton.
- Insulin stimulation of phosphorylation of the beta subunit of the insulin receptor. Formation of both phosphoserine and phosphotyrosine.
- Self-phosphorylation enhances the protein-tyrosine kinase activity of the epidermal growth factor receptor.
- Tyrosine phosphorylation of insulin receptor beta subunit activates the receptor tyrosine kinase in intact H-35 hepatoma cells.
- C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity.
Cited by
- Protein phosphorylation: a motive force for adaptive evolution.
- Activation of CD4 cells by fibronectin and anti-CD3 antibody. A synergistic effect mediated by the VLA-5 fibronectin receptor complex
- The guanylate cyclase/receptor family of proteins
- Interactions between the Methylation Sites of the Escherichia coli Aspartate Receptor Mediated by the Methyltransferase (*)
- Novel regulation of muscarinic receptors and their coupling with G proteins in smooth muscle: transient resensitization during desensitizing process
- Identification of a Motif in the Carboxyl Terminus of β-Arrestin2 Responsible for Activation of JNK3*
- G-protein-coupled Receptor (GPCR) Kinase Phosphorylation and β-Arrestin Recruitment Regulate the Constitutive Signaling Activity of the Human Cytomegalovirus US28 GPCR*
- Structure of the lutropin/choriogonadotropin receptor.
- Arrestin interactions with G protein-coupled receptors.
- Function of the antigen receptor in T cell activation.
- Characterization of the phosphorylation state of natriuretic peptide receptor-C
- Agonist receptors and G proteins as mediators of platelet activation.
- Glycoprotein IIIa is phosphorylated in intact human platelets.
- Gonadotropin-releasing hormone receptors: structure, expression, and signaling transduction.
- Molecular biology of receptors for neuropeptide hormones.
- MODELLING β2AR REGULATION
- Are lymphocytes excitable cells?
- Metabolic control of glucose degradation in yeast and tumor cells.
- Stimulation by auxin of phospholipase A in membrane vesicles from an auxin-sensitive tissue is mediated by an auxin receptor
- Ionic Channels and Effect of Taurine on the Heart
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