Search our Database of Scientific Publications and Authors

I’m looking for a

    Details and Download Full Text PDF:
    Activation of signaling receptors: do ligands bind to receptor monomer, dimer, or both?

    BMC Biophys 2013 Jun 3;6. Epub 2013 Jun 3.
    Department of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA.
    A recent study by Dietz et al. using single-molecule fluorescence microscopy techniques demonstrates that, in the absence of the ligand InlB, the MET receptor exists as both a monomer and a dimer on the cell membrane, and addition of the ligand leads to increased MET dimerization. Under the crowded conditions of the cell membrane, dimer formation may be a common phenomenon for cell surface receptors. Ligand binding to both monomeric and dimeric receptors may provide parallel routes to receptor activation.
    PDF Download - Full Text Link
    ( Please be advised that this article is hosted on an external website not affiliated with
    Source Status ListingPossible

    Similar Publications

    Structural basis of MET receptor dimerization by the bacterial invasion protein InlB and the HGF/SF splice variant NK1.
    Biochim Biophys Acta 2013 Oct 31;1834(10):2195-204. Epub 2012 Oct 31.
    Department of Chemistry and Center for Biotechnology (CeBiTec), Bielefeld University, 33501 Bielefeld, Germany. Electronic address:
    The structural basis of ligand-induced dimerization of the receptor tyrosine kinase MET by its natural ligand hepatocyte growth factor/scatter factor (HGF/SF) is not well understood. However, interesting insight into the molecular mechanism of MET dimerization has emerged from crystal structures of MET in complex with a bacterial agonist, the invasion protein internalin B (InlB) from pathogenic Listeria monocytogenes. MET activation by InlB promotes uptake of bacteria into host cells. Read More
    The PH domain of phosphoinositide-dependent kinase-1 exhibits a novel, phospho-regulated monomer-dimer equilibrium with important implications for kinase domain activation: single-molecule and ensemble studies.
    Biochemistry 2013 Jul 9;52(28):4820-9. Epub 2013 Jul 9.
    Department of Chemistry and Biochemistry and Molecular Biophysics Program, University of Colorado , Boulder, Colorado 80309-0596, United States.
    Phosphoinositide-dependent kinase-1 (PDK1) is an essential master kinase recruited to the plasma membrane by the binding of its C-terminal PH domain to the signaling lipid phosphatidylinositol-3,4,5-trisphosphate (PIP3). Membrane binding leads to PDK1 phospho-activation, but despite the central role of PDK1 in signaling and cancer biology, this activation mechanism remains poorly understood. PDK1 has been shown to exist as a dimer in cells, and one crystal structure of its isolated PH domain exhibits a putative dimer interface. Read More
    Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A multidimensional microscopy analysis.
    J Biol Chem 2005 Aug 30;280(34):30392-9. Epub 2005 Jun 30.
    Ludwig Institute for Cancer Research, Melbourne Tumour Biology Branch, Royal Melbourne Hospital, Victoria 3050, Australia.
    The epidermal growth factor receptor (EGFR) is a member of the erbB tyrosine kinase family of receptors. For many years it has been believed that receptor activation occurs via a monomer-dimer transition that is associated with a conformational change to activate the kinase. However, little is known about the quaternary state of the receptor at normal levels of expression (<10(5) receptors/cell). Read More
    Ligand-induced dimerization of the platelet-derived growth factor receptor. Monomer-dimer interconversion occurs independent of receptor phosphorylation.
    J Biol Chem 1989 Jul;264(20):11699-705
    Division of Oncology, Children's Hospital of Philadelphia, Pennsylvania 19104.
    The platelet-derived growth factor (PDGF) receptor is a single membrane-spanning polypeptide of 180,000 daltons with a ligand-stimulatable tyrosine kinase site. We have investigated changes in the structure and association state of the receptor that are induced by ligand binding, but which precede autophosphorylation. Chemical cross-linking of PDGF-bound 32P-labeled receptor and 125I-PDGF-labeled receptor resulted in the generation of a radiolabeled cross-linked complex of 370-390 kDa. Read More