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General structural features that regulate integrin affinity revealed by atypical αVβ8.

Jianchuan Wang1,2, Yang Su1,2, Roxana E Iacob3

  • 1Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.

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Summary
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Integrin αVβ8 exhibits unique structural features that enable ligand binding without large conformational changes, unlike integrin αVβ6. These differences in integrin structure and dynamics control TGF-β activation affinity.

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Area of Science:

  • Molecular and Structural Biology
  • Cellular Adhesion Mechanisms
  • Protein Dynamics and Interactions

Background:

  • Integrins are crucial cell surface receptors involved in cell adhesion and signaling.
  • Integrin αVβ8 and αVβ6 activate latent transforming growth factor-betas (TGF-βs), but αVβ8 has atypical properties.
  • Understanding integrin structural dynamics is key to deciphering their function in biological processes.

Purpose of the Study:

  • To structurally and dynamically compare integrin αVβ8 with αVβ6.
  • To elucidate the molecular mechanisms underlying the distinct ligand-binding affinities of αVβ8 and αVβ6.
  • To identify key structural features that regulate integrin affinity and signaling.

Main Methods:

  • Crystal structure determination of integrins.
  • Hydrogen-deuterium exchange mass spectrometry (HDX-MS) to probe protein dynamics.
  • Site-directed mutagenesis and affinity measurements to assess functional impact.

Main Results:

  • Integrin αVβ8 lacks a divalent cation binding site and possesses a unique β6-α7 loop conformation, facilitating high-affinity states.
  • Unlike other integrins, αVβ8's ligand binding involves α1/α1' helix movements without significant β6-α7 loop reshaping or α7-helix pistoning.
  • Reciprocal βI domain swaps between αVβ6 and αVβ8 demonstrated that these domains regulate affinity and coupling to the hybrid domain.

Conclusions:

  • Integrin αVβ8's atypical structure allows for efficient TGF-β activation through unique conformational dynamics.
  • Specific structural elements within the βI domain and its coupling to the hybrid domain are critical determinants of integrin affinity.
  • These findings provide insights into integrin structure-function relationships and their roles in TGF-β signaling pathways.