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    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.

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    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
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    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