Mechanism of Homophilic Adhesion by the Neural Cell Adhesion Molecule: Use of Multiple Domains and Flexibility
The extracellular regions of adhesion proteins of the Ig superfamily comprise multiple, tandemly arranged domains. We used direct-force measurements to investigate how this modular architecture contributes to the adhesive interactions of the neural cell adhesion molecule (NCAM), a representative of...
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| Published in: | Proceedings of the National Academy of Sciences - PNAS Vol. 101; no. 18; pp. 6963 - 6968 |
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| Format: | Journal Article |
| Language: | English |
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04-05-2004
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| Abstract | The extracellular regions of adhesion proteins of the Ig superfamily comprise multiple, tandemly arranged domains. We used direct-force measurements to investigate how this modular architecture contributes to the adhesive interactions of the neural cell adhesion molecule (NCAM), a representative of this protein class. The extracellular region of NCAM comprises five immunoglobulin and two fibronectin domains. Previous investigations generated different models for the mechanism of homophilic adhesion that each use different domains. We use force measurements to demonstrate that NCAM binds in two spatially distinct configurations. Ig-domain deletion mutants identified the domains responsible for each of the adhesive bonds. The measurements also confirmed the existence of a flexible hinge that alters the orientation of the adhesive complexes and the intermembrane distance. These results suggest that a combination of multiple bound states and internal molecular flexibility allows for sequentially synergistic bond formation and the ability to accommodate differences in intercellular space. |
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| AbstractList | The extracellular regions of adhesion proteins of the Ig superfamily comprise multiple, tandemly arranged domains. We used directforce measurements to investigate how this modular architecture contributes to the adhesive interactions of the neural cell adhesion molecule (NCAM), a representative of this protein class. The extracellular region of NCAM comprises five immunoglobulin and two fibronectin domains. Previous investigations generated different models for the mechanism of homophilic adhesion that each use different domains. We use force measurements to demonstrate that NCAM binds in two spatially distinct configurations. Igdomain deletion mutants identified the domains responsible for each of the adhesive bonds. The measurements also confirmed the existence of a flexible hinge that alters the orientation of the adhesive complexes and the intermembrane distance. These results suggest that a combination of multiple bound states and internal molecular flexibility allows for sequentially synergistic bond formation and the ability to accommodate differences in intercellular space. The extracellular regions of adhesion proteins of the Ig superfamily comprise multiple, tandemly arranged domains. We used direct-force measurements to investigate how this modular architecture contributes to the adhesive interactions of the neural cell adhesion molecule (NCAM), a representative of this protein class. The extracellular region of NCAM comprises five immunoglobulin and two fibronectin domains. Previous investigations generated different models for the mechanism of homophilic adhesion that each use different domains. We use force measurements to demonstrate that NCAM binds in two spatially distinct configurations. Ig-domain deletion mutants identified the domains responsible for each of the adhesive bonds. The measurements also confirmed the existence of a flexible hinge that alters the orientation of the adhesive complexes and the intermembrane distance. These results suggest that a combination of multiple bound states and internal molecular flexibility allows for sequentially synergistic bond formation and the ability to accommodate differences in intercellular space. The extracellular regions of adhesion proteins of the Ig superfamily comprise multiple, tandemly arranged domains. We used directforce measurements to investigate how this modular architecture contributes to the adhesive interactions of the neural cell adhesion molecule (NCAM), a representative of this protein class. The extracellular region of NCAM comprises five immunoglobulin and two fibronectin domains. Previous investigations generated different models for the mechanism of homophilic adhesion that each use different domains. We use force measurements to demonstrate that NCAM binds in two spatially distinct configurations. Igdomain deletion mutants identified the domains responsible for each of the adhesive bonds. The measurements also confirmed the existence of a flexible hinge that alters the orientation of the adhesive complexes and the intermembrane distance. These results suggest that a combination of multiple bound states and internal molecular flexibility allows for sequentially synergistic bond formation and the ability to accommodate differences in intercellular space. [PUBLICATION ABSTRACT] |
| Author | Johnson, C. P. Schowalter, William R. Perrin-Tricaud, C. Fujimoto, I. Rutishauser, U. Leckband, D. |
| AuthorAffiliation | Departments of Chemistry and ‡ Chemical and Biomolecular Engineering and § Center for Biophysics and Computational Biology, University of Illinois at Urbana–Champaign, 600 South Mathews Avenue, Urbana, IL 61801; and † Cell Biology Program, Memorial Sloan–Kettering Cancer Center, 1275 York Avenue, New York, NY 10021 |
| AuthorAffiliation_xml | – name: Departments of Chemistry and ‡ Chemical and Biomolecular Engineering and § Center for Biophysics and Computational Biology, University of Illinois at Urbana–Champaign, 600 South Mathews Avenue, Urbana, IL 61801; and † Cell Biology Program, Memorial Sloan–Kettering Cancer Center, 1275 York Avenue, New York, NY 10021 |
| Author_xml | – sequence: 1 givenname: C. P. surname: Johnson fullname: Johnson, C. P. – sequence: 2 givenname: I. surname: Fujimoto fullname: Fujimoto, I. – sequence: 3 givenname: C. surname: Perrin-Tricaud fullname: Perrin-Tricaud, C. – sequence: 4 givenname: U. surname: Rutishauser fullname: Rutishauser, U. – sequence: 5 givenname: D. surname: Leckband fullname: Leckband, D. – sequence: 6 givenname: William R. surname: Schowalter fullname: Schowalter, William R. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/15118102$$D View this record in MEDLINE/PubMed |
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| Copyright | Copyright 1993/2004 The National Academy of Sciences of the United States of America Copyright National Academy of Sciences May 4, 2004 Copyright © 2004, The National Academy of Sciences 2004 |
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| Notes | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 To whom correspondence should be addressed. E-mail: leckband@scs.uiuc.edu. Communicated by William R. Schowalter, Princeton University, Princeton, NJ, December 3, 2003 Abbreviations: NCAM, neural cell adhesion molecule; Fn, fibronectin; SPR, surface plasmon resonance; SFA, surface force apparatus. |
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| Snippet | The extracellular regions of adhesion proteins of the Ig superfamily comprise multiple, tandemly arranged domains. We used direct-force measurements to... The extracellular regions of adhesion proteins of the Ig superfamily comprise multiple, tandemly arranged domains. We used directforce measurements to... The extracellular regions of adhesion proteins of the Ig superfamily comprise multiple, tandemly arranged domains. We used direct force measurements to... |
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| SubjectTerms | Adhesion Adhesive bonding Adhesives Amino acids Animals Biological Sciences Biophysics Cell adhesion Cell Adhesion - physiology Chemical bonding CHO Cells Cricetinae Lipid Bilayers - metabolism Lipids Modeling Neural cell adhesion molecules Neural Cell Adhesion Molecules - metabolism Protein Structure, Tertiary Proteins |
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| Title | Mechanism of Homophilic Adhesion by the Neural Cell Adhesion Molecule: Use of Multiple Domains and Flexibility |
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