Epidermal Growth Factor Receptor Dimerization and Activation Require Ligand-Induced Conformational Changes in the Dimer Interface
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Published in | Molecular and Cellular Biology Vol. 25; no. 17; pp. 7734 - 7742 |
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Format | Journal Article |
Language | English |
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American Society for Microbiology
01.09.2005
Taylor & Francis |
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AbstractList | Structural studies have shown that ligand-induced epidermal growth factor receptor (EGFR) dimerization involves major domain rearrangements that expose a critical dimerization arm. However, simply exposing this arm is not sufficient for receptor dimerization, suggesting that additional ligand-induced dimer contacts are required. To map these contributions to the dimer interface, we individually mutated each contact suggested by crystallographic studies and analyzed the effects on receptor dimerization, activation, and ligand binding. We find that domain II contributes >90% of the driving energy for dimerization of the extracellular region, with domain IV adding little. Within domain II, the dimerization arm forms much of the dimer interface, as expected. However, a loop from the sixth disulfide-bonded module (immediately C-terminal to the dimerization arm) also makes a critical contribution. Specific ligand-induced conformational changes in domain II are required for this loop to contribute to receptor dimerization, and we identify a set of ligand-induced intramolecular interactions that appear to be important in driving these changes, effectively "buttressing" the dimer interface. Our data also suggest that similar conformational changes may determine the specificity of ErbB receptor homo- versus heterodimerization. Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MCB .asm.org, visit: MCB Structural studies have shown that ligand-induced epidermal growth factor receptor (EGFR) dimerization involves major domain rearrangements that expose a critical dimerization arm. However, simply exposing this arm is not sufficient for receptor dimerization, suggesting that additional ligand-induced dimer contacts are required. To map these contributions to the dimer interface, we individually mutated each contact suggested by crystallographic studies and analyzed the effects on receptor dimerization, activation, and ligand binding. We find that domain II contributes >90% of the driving energy for dimerization of the extracellular region, with domain IV adding little. Within domain II, the dimerization arm forms much of the dimer interface, as expected. However, a loop from the sixth disulfide-bonded module (immediately C-terminal to the dimerization arm) also makes a critical contribution. Specific ligand-induced conformational changes in domain II are required for this loop to contribute to receptor dimerization, and we identify a set of ligand-induced intramolecular interactions that appear to be important in driving these changes, effectively "buttressing" the dimer interface. Our data also suggest that similar conformational changes may determine the specificity of ErbB receptor homo- versus heterodimerization. |
Author | Jessica P. Dawson Chun-Chi Lin Mitchell B. Berger Mark A. Lemmon Kathryn M. Ferguson Joseph Schlessinger |
AuthorAffiliation | Department of Biochemistry and Biophysics, 1 Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania, 2 Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 3 |
AuthorAffiliation_xml | – name: Department of Biochemistry and Biophysics, 1 Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania, 2 Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 3 |
Author_xml | – sequence: 1 givenname: Jessica P. surname: Dawson fullname: Dawson, Jessica P. organization: Department of Biochemistry and Biophysics – sequence: 2 givenname: Mitchell B. surname: Berger fullname: Berger, Mitchell B. organization: Department of Biochemistry and Biophysics – sequence: 3 givenname: Chun-Chi surname: Lin fullname: Lin, Chun-Chi organization: Department of Physiology, University of Pennsylvania School of Medicine – sequence: 4 givenname: Joseph surname: Schlessinger fullname: Schlessinger, Joseph organization: Department of Pharmacology, Yale University School of Medicine – sequence: 5 givenname: Mark A. surname: Lemmon fullname: Lemmon, Mark A. email: mlemmon@mail.med.upenn.edu organization: Department of Biochemistry and Biophysics – sequence: 6 givenname: Kathryn M. surname: Ferguson fullname: Ferguson, Kathryn M. organization: Department of Physiology, University of Pennsylvania School of Medicine |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16107719$$D View this record in MEDLINE/PubMed |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Corresponding author. Mailing address: Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, 809C Stellar-Chance Laboratories, 422 Curie Boulevard, Philadelphia, PA 19104-6059. Phone: (215) 898-3072. Fax: (215) 573-4764. E-mail: mlemmon@mail.med.upenn.edu. J.P.D. and M.B.B. contributed equally to this study. |
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Mendeley... Structural studies have shown that ligand-induced epidermal growth factor receptor (EGFR) dimerization involves major domain rearrangements that expose a... |
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SubjectTerms | Binding Sites Dimerization Enzyme Activation Ligands Models, Molecular Molecular Sequence Data Mutation - genetics Protein Structure, Quaternary Protein Structure, Tertiary Receptor, Epidermal Growth Factor - chemistry Receptor, Epidermal Growth Factor - genetics Receptor, Epidermal Growth Factor - metabolism Signal Transduction Surface Plasmon Resonance Transforming Growth Factor alpha - pharmacology |
Title | Epidermal Growth Factor Receptor Dimerization and Activation Require Ligand-Induced Conformational Changes in the Dimer Interface |
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