Structural basis of adhesion‐molecule recognition by ERM proteins revealed by the crystal structure of the radixin—ICAM‐2 complex
Open accessAbstract
ERM (ezrin/radixin/moesin) proteins recognize the cytoplasmic domains of adhesion molecules in the formation of the membrane-associated cytoskeleton. Here we report the crystal structure of the radixin FERM (4.1 and ERM) domain complexed with the ICAM-2 cytoplasmic peptide. The non-polar region of the ICAM-2 peptide contains the RxxTYxVxxA sequence motif to form a beta-strand followed by a short 3(10)-helix. It binds the groove of the phosphotyrosine-binding (PTB)-like subdomain C mediated by a beta-beta association and several side-chain interactions. The binding mode of the ICAM-2 peptide to the FERM domain is distinct from that of the NPxY motif-containing peptide binding to the canonical PTB domain. Mutation analyses based on the crystal structure reveal the determinant elements of recognition and provide the first insights into the physical link between adhesion molecules and ERM proteins.
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The interaction interface between several FERM domains and their cognate membrane-protein substrates has been resolved by atomic resolution.
“The interaction interface between several FERM domains and their cognate membrane-protein substrates has been resolved by atomic resolution (22,23).”
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Research works printed but not linked: 3
- Dhe-Paganon,S., Ottinger,E.A., Nolte,R.T., Eck,M.J. and Shoelson,S.E. (1999) Crystal structure of the pleckstrin homology±phosphotyrosine binding (PH±PTB) targeting region of insulin receptor substrate 1. Proc. Natl Acad. Sci. USA, 96, 8378±8383.
- Pearson,M.A., Reczek,D., Bretscher,A. and Karplus,P.A. (2000) Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell, 101, 259±270.
- Schultz,J., Milpetz,F., Bork,P. and Ponting,C.P. (1998) SMART, a simple modular architecture research tool: identi®cation of signaling domains. Proc. Natl Acad. Sci. USA, 95, 5857±5864.
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Sorrentino, V., Scheer, L., Santos, A., Reits, E., Bleijlevens, B., & Zelcer, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.249557 · Cited by 53 · see citing works
- Authors
- Hamada, K., Shimizu, T., Yonemura, S., Tsukita, S., Tsukita, S., & Hakoshima, T.
- Affiliations
- SPring-8 (JP)
- Nara Institute of Science and Technology (JP)
- Kyoto University (JP)
- Corresponding author
- Hakoshima, Toshio
- Venue
- The EMBO Journal
- Published
- 2003-02-03
- Volume
- 22
- Issue
- 3
- Pages
- 502-514
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC140724
- OpenAlex
- W2039771278
- Cited by
- 155
- References
- 0
- Citations by year
- 2026: 2 · 2024: 2 · 2023: 5 · 2022: 2 · 2021: 4 · 2020: 4 · 2019: 4 · 2018: 4 · 2017: 6 · 2016: 6 · 2015: 5 · 2014: 6 · 2013: 7 · 2012: 5
- FWCI
- 7.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- Funders
- Japan Society for the Promotion of Science (12490024, 10359003, 10179103)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- ERM proteins, radixin, FERM domain, ICAM-2, phosphotyrosine binding domain, peptide binding, beta-strand, 310-helix, binding determinants
- MeSH terms
- Amino Acid Sequence, Animals, Blood Proteins, Cell Membrane, Cytoskeletal Proteins, Cytoskeleton, Humans, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Mutation, Peptides, Protein Binding, Molecular Structure, Trans-Activators, Antigens, CD, Cell Adhesion Molecules, Sequence Alignment, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Macromolecular Substances, beta Catenin, Mice
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