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Related Experiment Videos

CD98 modulates integrin beta1 function in polarized epithelial cells.

Songmin Cai1, Nada Bulus, Priscila M Fonseca-Siesser

  • 1Division of Nephrology, Department of Medicine, Vanderbilt University Medical Center, 1161 21st Avenue South, Nashville, TN 37232, USA.

Journal of Cell Science
|February 17, 2005
PubMed
Summary
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The transmembrane protein CD98 is crucial for cell adhesion and migration in kidney cells. Its transmembrane domain, specifically the N-terminal amino acids, mediates interactions with beta1 integrins, influencing cell functions.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • CD98 (collectin-11) is a type II transmembrane protein and the heavy chain of heterodimeric amino acid transporters (HAT).
  • CD98 is essential for surface expression and basolateral localization of HAT in polarized epithelial cells.
  • CD98 interacts with beta1 integrins, enhancing their ligand affinity.

Purpose of the Study:

  • To investigate the role of CD98's transmembrane and cytoplasmic domains in integrin-dependent cell adhesion and migration.
  • To elucidate the specific CD98 domains and interactions critical for these cellular processes in polarized renal epithelial cells.

Main Methods:

  • Utilized mutant CD98 constructs lacking cytoplasmic tails or specific transmembrane domain amino acids.
  • Assessed cell adhesion, migration, focal adhesion formation, and FAK/AKT phosphorylation.

Related Experiment Videos

  • Employed phosphoinositol 3-OH kinase (PI3-K) inhibitors to evaluate pathway dependency.
  • Examined branching morphogenesis in collagen gels.

    • Main Results:

    • The CD98 transmembrane domain alone was sufficient for beta1 integrin interaction; five N-terminal amino acids were essential.
    • Overexpression of full-length CD98 or CD98 lacking its tail enhanced cell adhesion and migration.
    • Deletion of the critical transmembrane amino acids abrogated these effects.
    • CD98 interaction with beta1 integrins increased focal adhesion formation and FAK/AKT phosphorylation, dependent on PI3-K.
    • CD98 modulated polarized renal epithelial cell branching morphogenesis.

    Conclusions:

    • CD98 acts as a scaffolding protein in polarized renal epithelial cells.
    • It interacts with both amino acid transporters and beta1 integrins.
    • CD98 influences diverse cellular functions including amino acid transport, cell adhesion, migration, and branching morphogenesis.