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Cited by 131Cell Adhesion Molecules ResearchProtein Structure and DynamicsBiochemical and Structural Characterization

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The Structure of an Interdomain Complex That Regulates Talin Activity

Open access
Goult, Benjamin T., Bate, Neil, Anthis, Nicholas J., Wegener, Kate L., Gingras, Alexandre R., Patel, Bipin, Barsukov, Igor L., Campbell, Iain D., Roberts, Gordon C.K., Critchley, David R.·2009·Journal of Biological Chemistry
DOI 10.1074/jbc.m900078200PMC PMC2685691
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Abstract

Talin is a large flexible rod-shaped protein that activates the integrin family of cell adhesion molecules and couples them to cytoskeletal actin. It exists in both globular and extended conformations, and an intramolecular interaction between the N-terminal F3 FERM subdomain and the C-terminal part of the talin rod contributes to an autoinhibited form of the molecule. Here, we report the solution structure of the primary F3 binding domain within the C-terminal region of the talin rod and use intermolecular nuclear Overhauser effects to determine the structure of the complex. The rod domain (residues 1655-1822) is an amphipathic five-helix bundle; Tyr-377 of F3 docks into a hydrophobic pocket at one end of the bundle, whereas a basic loop in F3 (residues 316-326) interacts with a cluster of acidic residues in the middle of helix 4. Mutation of Glu-1770 abolishes binding. The rod domain competes with beta3-integrin tails for binding to F3, and the structure of the complex suggests that the rod is also likely to sterically inhibit binding of the FERM domain to the membrane.

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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).”

    From Distinct Functional Domains Contribute to Degradation of the Low Density Lipoprotein Receptor (LDLR) by the E3 Ubiquitin Ligase Inducible Degrader of the LDLR (IDOL) (2011) · cites this paper as [22]

    The Abstract and Results describe a structural model of the interface between talin’s F3 FERM subdomain and a domain of the talin rod. They do not report structures of several FERM domains bound to their cognate membrane-protein substrates; the Discussion instead compares this complex with a previously determined F3–integrin-tail complex. No page numbers are available in our copy. (LLM, conf=0.84)

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Metadata

Authors
Goult, B. T., Bate, N., Anthis, N. J., Wegener, K. L., Gingras, A. R., Patel, B., Barsukov, I. L., Campbell, I. D., Roberts, G. C. K., & Critchley, D. R.
Affiliations
  • University of Leicester (GB)
  • University of Oxford (GB)
  • University of Liverpool (GB)
Corresponding author
Critchley, David R.
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2009-05
Volume
284
Issue
22
Pages
15097-15106
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.m900078200
PMC
PMC2685691
OpenAlex
W2162005182
Cited by
131
References
4
Citations by year
2026: 5 · 2025: 3 · 2024: 6 · 2023: 4 · 2022: 3 · 2021: 7 · 2020: 12 · 2019: 7 · 2018: 5 · 2017: 9 · 2016: 9 · 2015: 8 · 2014: 8 · 2013: 8 · 2012: 13
FWCI
9.33
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion)
  • Kent Academic Repository (University of Kent) (submittedVersion)
  • Leicester Research Archive (University of Leicester) (submittedVersion)
Funders
  • Wellcome Trust
  • Cancer Research UK
  • National Institutes of Health (5u54gm064346-10, GM-64346, U54 GM64346)
  • National Institute of General Medical Sciences (U54 GM 64346)
Topics
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Keywords
talin, integrin activation, CD61, autoinhibition, protein-protein complex structure, nuclear Overhauser effect, actin cytoskeleton, cell adhesion, solution structure
MeSH terms
Amino Acid Sequence, Animals, Binding Sites, Models, Molecular, Molecular Sequence Data, Mutation, Magnetic Resonance Spectroscopy, Protein Binding, Solutions, Talin, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Interaction Mapping, Integrin beta3, Mutant Proteins, Mice

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