Mechanisms of Activation of Receptor Tyrosine Kinases: Monomers or Dimers
- Biology, ChemistryCells
Two mutually exclusive models for the mechanisms of activation of the epidermal growth factor receptor, the neurotrophin receptor and IR families are discussed based on new insights.
Cytokine and growth factor receptors in the nucleus: What's up with that?
- BiologyJournal of cellular biochemistry
How close the authors are to demonstrating that direct translocation of receptors, or receptor fragments, from the cell surface to the nucleus is a physiologically relevant means of intracellular signaling that can supplant or complement canonical signaling cascades is examined.
Cell-Surface Receptors Transactivation Mediated by G Protein-Coupled Receptors
- BiologyInternational journal of molecular sciences
The main mechanisms of G PCR-mediated cell-surface receptors transactivation and the pathways involved in intracellular responses induced by GPCR agonists are discussed to suggest the design of novel strategies for therapeutic interventions.
Transmembrane peptides as inhibitors of ErbB receptor signaling.
- BiologyMolecular biology of the cell
Mechanism of action involves inhibition of dimerization of the receptors as shown by the lack of effects of mutant nondimerizing sequences, completed by density centrifugation and covalent cross-linking experiments.
Diversity of receptor tyrosine kinase signaling mechanisms
- Biology, Chemistry
A model for ligand-induced ALK dimerization and activation is proposed, and efforts to understand the molecular mechanisms of Drl/DWnt5 binding suggest that DWnt5 may interact with Drl through a binding mode that differs from Wnt binding to other receptors.
Receptor tyrosine kinase signaling mechanisms: Devolving TrkA responses with phosphoproteomics.
- BiologyAdvances in biological regulation
structural on the regulation of the epidermal growth factor receptor.
- Biology, Chemistry
The epidermal growth factor receptor is a receptor tyrosine kinase that plays a critical role in the pathogenesis of many cancers, and intense investigations of fragments of this receptor have provided a detailed view of its activation mechanism, which is reviewed here.
Biological function of nuclear receptor tyrosine kinase action.
- BiologyCold Spring Harbor perspectives in biology
The identification of this novel signaling mechanism calls for a critical reevaluation of the mechanisms of action of RTKs and their biological roles.
HER2 Transmembrane Domain Dimerization Coupled with Self-Association of Membrane-Embedded Cytoplasmic Juxtamembrane Regions.
- Biology, ChemistryJournal of molecular biology
SHOWING 1-10 OF 125 REFERENCES
Secondary Dimerization between Members of the Epidermal Growth Factor Receptor Family*
- BiologyThe Journal of Biological Chemistry
Evidence is provided for a new mechanism for growth factor-stimulated receptor dimer formation, designated secondary dimerization, and points to a novel mechanism by which multiple signaling activities and diverse biological responses are initiated by members of the EGF receptor family.
LAT The ZAP-70 Tyrosine Kinase Substrate that Links T Cell Receptor to Cellular Activation
The ErbB signaling network: receptor heterodimerization in development and cancer
- BiologyThe EMBO journal
The role of ErbB receptors as normal signal transducers and their contribution to the process of malignant transformation during tumor development are concentrated on.
Employment of the Epidermal Growth Factor Receptor in Growth Factor–Independent Signaling Pathways
- BiologyThe Journal of cell biology
The data not only show EGF-independent tyrosine phosphorylation of the EGF receptor, but also provide experimental evidence that the E GF receptor participates in the signaling events and cellular responses initiated by these various stimuli.
Heterodimerization of epidermal growth factor receptor and wild-type or kinase-deficient Neu: a mechanism of interreceptor kinase activation and transphosphorylation.
- Biology, Computer ScienceProceedings of the National Academy of Sciences of the United States of America
Results provided evidence that the Neu ectodomain is sufficient to associate with EGFR physically, and the cytoplasmic domain interaction is required for heterodimeric kinase activation, indicating that Neu/c-erbB2 is not just a simple substrate for EGFR but a transactivator as well.
Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1
- Biology, Computer ScienceMolecular and cellular biology
The notion that IRS-1 is a multisite docking protein that engages various downstream regulatory elements during insulin signal transmission is extended, as the p85 alpha recognizes YMXM motifs and suggest that GRB2 prefers a phosphorylated YVNI motif, whereas SHPTP2 (Syp) binds to a phosphORYlated YIDL motif.
PH Domains: Diverse Sequences with a Common Fold Recruit Signaling Molecules to the Cell Surface
Signal-dependent membrane targeting by pleckstrin homology (PH) domains.
- BiologyThe Biochemical journal
The possibility that membrane targeting by PH domains with low affinity for phosphoinositides could be driven by alteration of their oligomeric state and thus the avidity of their membrane binding is discussed.