Integrin α3β1 Binding to Fibronectin Is Dependent on the Ninth Type III Repeat.

The Journal of Biological Chemistry
Ashley C BrownThomas H Barker

Abstract

Fibronectin (Fn) is a promiscuous ligand for numerous cell adhesion receptors or integrins. The vast majority of Fn-integrin interactions are mediated through the Fn Arg-Gly-Asp (RGD) motif located within the tenth type III repeat. In the case of integrins αIIbβ3 and α5β1, the integrin binds RGD and the synergy site (PHSRN) located within the adjacent ninth type III repeat. Prior work has shown that these synergy-dependent integrins are exquisitely sensitive to perturbations in the Fn integrin binding domain conformation. Our own prior studies of epithelial cell responses to recombinant fragments of the Fn integrin binding domain led us to hypothesize that integrin α3β1 binding may also be modulated by the synergy site. To explore this hypothesis, we created a variety of recombinant variants of the Fn integrin binding domain: (i) a previously reported (Leu → Pro) stabilizing mutant (FnIII9'10), (ii) an Arg to Ala synergy site mutation (FnIII9(R)→(A)10), (iii) a two-Gly (FnIII9(2G)10) insertion, and (iv) a four-Gly (FNIII9(4G)10) insertion in the interdomain linker region and used surface plasmon resonance to determine binding kinetics of integrin α3β1 to the Fn fragments. Integrin α3β1 had the highest affinity for FnIII9'10 and...Continue Reading

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Citations

Mar 26, 2016·Biochemistry·Tarik A KhanJennifer A Maynard
Jul 15, 2017·Viruses·Martin Hufbauer, Baki Akgül
Sep 18, 2020·Advanced Healthcare Materials·Prachi DhavalikarElizabeth Cosgriff-Hernandez
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Apr 9, 2018·ACS Biomaterials Science & Engineering·Emily P Mihalko, Ashley C Brown
Nov 19, 2021·The Journal of Clinical Endocrinology and Metabolism·Hannah R NietoChristopher J McCabe

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