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Membrane Receptor Mapping: The Membrane Topography of FcεRI Signaling

  • Chapter
Membrane Dynamics and Domains

Part of the book series: Subcellular Biochemistry ((SCBI,volume 37))

Abstract

Ligand binding to membrane receptors initiates cascades of biochemical events leading to physiological responses. Hundreds of proteins and lipids are implicated in signaling networks and programs in genomics and proteomics are continuously adding new components to the signaling “parts lists”. Here, we generate high resolution maps of signaling networks using cytoplasmic face-up membrane sheets that can be labeled with inununogold probes (3–10 nm) and imaged in the transmission electron microscope. Our model system is the mast cell and we focus on mapping the topography of the high affinity IgE receptor, FcεRI, its associated tyrosine kinases, Lyn and Syk, and the signaling proteins that propagate signals from these kinases. Crosslinked receptors and their signaling partners segregate during signaling to multiple, dynamic membrane domains, including a transient FcεRI-Lyn domain and at least two other distinct domains, one characterized by the presence of receptor, Syk and multiple signaling proteins, but not Lyn (primary signaling domains), and one characterized by the presence of LAT and PLCγl but not receptor (secondary signaling domains). PI 3-kinase associates with both primary and secondary signaling domains and may help to recruit specific signaling proteins through the local remodeling of inositol phospholipids. The lipid raft markers, GM1 and Thy-1, fail to localize in native membrane sheets either with each other or with signaling domains. We introduce new probes to localize multiple signaling molecules on the same membrane sheet and new computational tools to capture and analyze their topographical relationships. In the future, we expect that high resolution maps of signaling networks will be integrated with chemical kinetic analyses, with cell fractionation data and with a range of real-time fluorescence measurements, into mathematical models with power to predict mechanisms that regulate the efficiency, specificity, amplitude and duration of signaling pathways.

Our colleague, Carla Wofsy, died on August 4, 2003, after a long illness. This chapter is dedicated to her memory as a pioneering mathematical biologist and as a human of enormous grace, integrity and compassion.

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Author notes

  1. Margaret L. Sanders

    Present address: Department of Family and Community Medicine, University of New Mexico, USA

Authors and Affiliations

  1. Department of Pathology, University of New Mexico, Albuquerque, NM, USA

    Janet M. Oliver, Janet R. Pfeiffer, Zurab Surviladze & Bridget S. Wilson

  2. Department of Mathematics and Statistics, University of New Mexico, Albuquerque, NM, USA

    Stanly L. Steinberg, Karin Leiderman, Margaret L. Sanders & Carla Wofsy

  3. Department of Computer Science, University of New Mexico, Albuquerque, NM, USA

    Jun Zhang

  4. Advanced Material Laboratory, Sandia National Laboratories, Albuquerque, NM, USA

    Hong You Fan, Nicholas Andrews, Scott Bunge & Timothy J. Boyle

  5. Materials Characterization Department, Materials and Process Center, Sandia National Laboratories, Albuquerque, NM, USA

    Paul Kotula

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  1. Janet M. Oliver
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Editors and Affiliations

  1. Department of Life Sciences, King’s College London, 150 Stamford Street, SE1 9NN, London, UK

    Peter J. Quinn

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Oliver, J.M. et al. (2004). Membrane Receptor Mapping: The Membrane Topography of FcεRI Signaling. In: Quinn, P.J. (eds) Membrane Dynamics and Domains. Subcellular Biochemistry, vol 37. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-5806-1_1

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