ArticleThe Journal of biological chemistry2003
Synergistic activity of the ninth and tenth FIII domains of human fibronectin depends upon structural stability.
Article in The Journal of biological chemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 35 citations in OpenAlex.
- Dynamics of integrin α5β1, fibronectin, and their complex reveal sites of interaction and conformational change.The Journal of biological chemistry · 2022Article
- Solubilization and Purification of αMethods in molecular biology (Clifton, N.J.) · 2022Article
- Nanomaterials can dynamically steer cell responses to biological ligands.Small (Weinheim an der Bergstrasse, Germany) · 2011Article
- Interaction of β-sheet folds with a gold surface.PloS one · 2011Article
- Collective cell migration on artificial extracellular matrix proteins containing full-length fibronectin domains.Advanced materials (Deerfield Beach, Fla.) · 2010Article
- Using self-assembled monolayers to model cell adhesion to the 9th and 10th type III domains of fibronectin.Langmuir : the ACS journal of surfaces and colloids · 2009Article
- The C-terminal region of laminin beta chains modulates the integrin binding affinities of laminins.The Journal of biological chemistry · 2009Article
- Assay to mechanically tune and optically probe fibrillar fibronectin conformations from fully relaxed to breakage.Matrix biology : journal of the International Society for Matrix Biology · 2008Article
- Interdomain tilt angle determines integrin-dependent function of the ninth and tenth FIII domains of human fibronectin.The Journal of biological chemistry · 2004Article
- Structure of the integrin binding fragment from fibrillin-1 gives new insights into microfibril organization.Structure (London, England : 1993) · 2004Article
- Structure of integrin alpha5beta1 in complex with fibronectin.The EMBO journal · 2003Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The ninth and tenth FIII domains (FIII9-10) of human fibronectin act in synergy to promote cell adhesion via the interaction with integrin receptors. Here we describe the functional and structural properties of a set of recombinant FIII9-10 mutants containing various alanine substitutions within the key synergistic site, DRVPHSRN in FIII9, either alone or in combination with another substitution (Leu(1408) to Pro), on the opposite face of FIII9, that increases stability and the functional capacity of FIII9-10. We show that the introduction of mutations into the synergistic sequence of FIII9-10 has a negative effect on the adhesion of baby hamster kidney fibroblasts and results in reduced ability of these ligands to recognize integrin alpha(5)beta(1). Conformational stability of the FIII9 domain in the synergy site mutants is likewise reduced in comparison with native FIII9. The Leu(1408) to Pro substitution in mutant FIII9-10 proteins carrying substitutions in the synergy site results in a substantial recovery of the adhesive activity of the mutants and affinity to alpha(5)beta(1). In keeping with the enhancement of functional activity, the Leu(1408) to Pro substitution in the FIII9-10 synergy site mutants also causes a significant increase in conformational stability of FIII9. These observations imply a strong positive correlation between the biological activity and conformational stability of the assessed FIII9-10 mutants and suggest that a Leu(1408) to Pro substitution restores the biological activity of the mutants via their ability to restore their conformational stability. We conclude that domain stability may be a major determinant of the synergistic potential of FIII9. Our data underscore the value of using more than one approach in such structure-function studies and the requirement for validating the global structural integrity of protein ligands in which sequences that disrupt function have been perturbed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.