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Related Experiment Videos

Minimum alpha chain cytoplasmic tail sequence needed to support integrin-mediated adhesion

P D Kassner1, S Kawaguchi, M E Hemler

  • 1Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115.

The Journal of Biological Chemistry
|August 5, 1994
PubMed
Summary
This summary is machine-generated.

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Short integrin tails restore cell adhesion. Adding a few amino acids after the GFFKR motif to integrin alpha chains significantly restores adhesive activity, with maximal function achieved using 5-7 amino acids.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Integrin alpha and beta subunits mediate cell adhesion.
  • Cytoplasmic domains of integrin alpha subunits are crucial for adhesive function.
  • Previous studies showed deletion of these domains abolishes VLA-4 and VLA-2 mediated adhesion.

Purpose of the Study:

  • To investigate the minimal amino acid sequence required for integrin alpha chain cytoplasmic domain function.
  • To determine the role of the cytoplasmic domain in divalent cation utilization and ligand binding.

Main Methods:

  • Expression of integrin alpha 4 and alpha 2 chains in MIP101 and Chinese hamster ovary cells.
  • Systematic addition of amino acids to the cytoplasmic domain after the GFFKR motif.
  • Divalent cation titration assays.

Related Experiment Videos

  • Cell adhesion assays with VCAM-1, CS1 peptide, and collagen.
  • Mutagenesis studies and domain swapping.
  • Assays in the presence of metabolic energy inhibitors and cell-free ligand binding assays.

    • Main Results:

    • Restoration of substantial adhesive activity with 3-4 amino acids and maximal activity with 5-7 amino acids added after the GFFKR motif.
    • Point mutations within the critical 5 alpha 4 residues did not affect adhesive activity.
    • Exchange of alpha 4 and alpha 2 tails did not alter function.
    • Deletion of cytoplasmic domains decreased divalent cation utilization efficiency.
    • Divalent cation effects were modulated by cation type/amount and cellular environment.
    • Deletion effects were minimal with metabolic inhibitors and absent in cell-free assays, suggesting intact intrinsic ligand interaction.

    Conclusions:

    • A short, non-specific stretch of amino acids in the integrin alpha chain cytoplasmic domain is sufficient for maximal adhesive activity.
    • Integrin cytoplasmic domains are critical for efficient divalent cation utilization in cell adhesion.
    • The cytoplasmic domain's primary role in adhesion may involve modulating cation-dependent conformational changes rather than direct ligand interaction.