Journal article
Binding Specificity of Multiprotein Signaling Complexes Is Determined by Both Cooperative Interactions and Affinity Preferences
Biochemistry (Easton), Vol.43(14), pp.4170-4178
04/01/2004
DOI: 10.1021/bi0357311
PMID: 15065860
Abstract
The generation of multiprotein complexes at receptors and adapter proteins is crucial for the activation of intracellular signaling pathways. In this study, we used multiple biochemical and biophysical methods to examine the binding properties of several SH2 and SH3 domain-containing signaling proteins as they interact with the adapter protein linker for activation of T-cells (LAT) to form multiprotein complexes. We observed that the binding specificity of these proteins for various LAT tyrosines appears to be constrained both by the affinity of binding and by cooperative protein-protein interactions. These studies provide quantitative information on how different binding parameters can determine in vivo binding site specificity observed for multiprotein signaling complexes.
Details
- Title: Subtitle
- Binding Specificity of Multiprotein Signaling Complexes Is Determined by Both Cooperative Interactions and Affinity Preferences
- Creators
- Jon C. D Houtman - Laboratory of Cellular and Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, and Protein Biophysics Resource, Division of Bioengineering and Physical Science, ORS, OD, National Institutes of Health, Bethesda, Maryland 20892, and Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850Yuichiro Higashimoto - Laboratory of Cellular and Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, and Protein Biophysics Resource, Division of Bioengineering and Physical Science, ORS, OD, National Institutes of Health, Bethesda, Maryland 20892, and Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850Nazzareno Dimasi - Laboratory of Cellular and Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, and Protein Biophysics Resource, Division of Bioengineering and Physical Science, ORS, OD, National Institutes of Health, Bethesda, Maryland 20892, and Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850Sangwoo Cho - Laboratory of Cellular and Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, and Protein Biophysics Resource, Division of Bioengineering and Physical Science, ORS, OD, National Institutes of Health, Bethesda, Maryland 20892, and Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850Hiroshi Yamaguchi - Laboratory of Cellular and Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, and Protein Biophysics Resource, Division of Bioengineering and Physical Science, ORS, OD, National Institutes of Health, Bethesda, Maryland 20892, and Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850Brent Bowden - Laboratory of Cellular and Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, and Protein Biophysics Resource, Division of Bioengineering and Physical Science, ORS, OD, National Institutes of Health, Bethesda, Maryland 20892, and Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850Carole Regan - Laboratory of Cellular and Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, and Protein Biophysics Resource, Division of Bioengineering and Physical Science, ORS, OD, National Institutes of Health, Bethesda, Maryland 20892, and Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850Emilio L Malchiodi - Laboratory of Cellular and Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, and Protein Biophysics Resource, Division of Bioengineering and Physical Science, ORS, OD, National Institutes of Health, Bethesda, Maryland 20892, and Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850Roy Mariuzza - Laboratory of Cellular and Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, and Protein Biophysics Resource, Division of Bioengineering and Physical Science, ORS, OD, National Institutes of Health, Bethesda, Maryland 20892, and Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850Peter Schuck - Laboratory of Cellular and Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, and Protein Biophysics Resource, Division of Bioengineering and Physical Science, ORS, OD, National Institutes of Health, Bethesda, Maryland 20892, and Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850Ettore Appella - Laboratory of Cellular and Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, and Protein Biophysics Resource, Division of Bioengineering and Physical Science, ORS, OD, National Institutes of Health, Bethesda, Maryland 20892, and Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850Lawrence E Samelson - Laboratory of Cellular and Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, and Protein Biophysics Resource, Division of Bioengineering and Physical Science, ORS, OD, National Institutes of Health, Bethesda, Maryland 20892, and Center for Advanced Research in Biotechnology, W. M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850
- Resource Type
- Journal article
- Publication Details
- Biochemistry (Easton), Vol.43(14), pp.4170-4178
- DOI
- 10.1021/bi0357311
- PMID
- 15065860
- ISSN
- 0006-2960
- eISSN
- 1520-4995
- Language
- English
- Date published
- 04/01/2004
- Academic Unit
- Microbiology and Immunology; Internal Medicine
- Record Identifier
- 9984094380302771
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