Paxillin binding to the alpha 4 integrin subunit stimulates LFA-1 (integrin alpha L beta 2)-dependent T cell migration by augmenting the activation of focal adhesion kinase/proline-rich tyrosine kinase-2

J Immunol. 2003 Jun 15;170(12):5912-8. doi: 10.4049/jimmunol.170.12.5912.

Abstract

Engagement of very late Ag-4 (integrin alpha(4)beta(1)) by ligands such as VCAM-1 markedly stimulates leukocyte migration mediated by LFA-1 (integrin alpha(L)beta(2)). This form of integrin trans-regulation in T cells requires the binding of paxillin to the alpha(4) integrin cytoplasmic domain. This conclusion is based on the abolition of trans-regulation in Jurkat T cells by an alpha(4) mutation (alpha(4)(Y991A)) that disrupts paxillin binding. Furthermore, cellular expression of an alpha(4)-binding fragment of paxillin that blocks the alpha(4)-paxillin interaction, selectively blocked VCAM-1 stimulation of alpha(L)beta(2)-dependent cell migration. The alpha(4)-paxillin association mediates trans-regulation by enhancing the activation of tyrosine kinases, focal adhesion kinase (FAK) and/or proline-rich tyrosine kinase-2 (Pyk2), based on two lines of evidence. First, disruption of the paxillin-binding site in the alpha(4) tail resulted in much less alpha(4)beta(1)-mediated phosphorylation of Pyk2 and FAK. Second, transfection with cDNAs encoding C-terminal fragments of Pyk2 and FAK, which block the function of the intact kinases, blocked alpha(4)beta(1) stimulation of alpha(L)beta(2)-dependent migration. These results define a proximal protein-protein interaction of an integrin cytoplasmic domain required for trans-regulation between integrins, and establish that augmented activation of Pyk2 and/or FAK is an immediate signaling event required for the trans-regulation of integrin alpha(L)beta(2) by alpha(4)beta(1).

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Substitution / genetics
  • Binding Sites / genetics
  • Cell Movement / genetics
  • Cell Movement / immunology*
  • Cytoplasm / metabolism
  • Cytoskeletal Proteins / metabolism*
  • Cytoskeletal Proteins / physiology
  • Enzyme Activation / genetics
  • Focal Adhesion Kinase 1
  • Focal Adhesion Kinase 2
  • Focal Adhesion Protein-Tyrosine Kinases
  • Humans
  • Integrin alpha4 / genetics
  • Integrin alpha4 / metabolism*
  • Integrin alpha4 / physiology
  • Integrin alpha4beta1 / antagonists & inhibitors
  • Integrin alpha4beta1 / genetics
  • Integrin alpha4beta1 / metabolism
  • Integrin alpha4beta1 / physiology
  • Jurkat Cells
  • Lymphocyte Function-Associated Antigen-1 / metabolism
  • Lymphocyte Function-Associated Antigen-1 / physiology*
  • Paxillin
  • Peptide Fragments / metabolism
  • Peptide Fragments / physiology
  • Phosphoproteins / metabolism*
  • Phosphoproteins / physiology
  • Protein Binding / genetics
  • Protein Structure, Tertiary / genetics
  • Protein Subunits / antagonists & inhibitors
  • Protein Subunits / genetics
  • Protein Subunits / metabolism
  • Protein Subunits / physiology
  • Protein-Tyrosine Kinases / antagonists & inhibitors
  • Protein-Tyrosine Kinases / genetics
  • Protein-Tyrosine Kinases / metabolism*
  • Protein-Tyrosine Kinases / physiology
  • Receptor Cross-Talk / physiology
  • Signal Transduction / genetics
  • Signal Transduction / immunology
  • T-Lymphocytes / cytology*
  • T-Lymphocytes / enzymology
  • T-Lymphocytes / metabolism*
  • Transfection
  • Vascular Cell Adhesion Molecule-1 / metabolism

Substances

  • Cytoskeletal Proteins
  • Integrin alpha4beta1
  • Lymphocyte Function-Associated Antigen-1
  • PXN protein, human
  • Paxillin
  • Peptide Fragments
  • Phosphoproteins
  • Protein Subunits
  • Vascular Cell Adhesion Molecule-1
  • Integrin alpha4
  • Protein-Tyrosine Kinases
  • Focal Adhesion Kinase 1
  • Focal Adhesion Kinase 2
  • Focal Adhesion Protein-Tyrosine Kinases
  • PTK2 protein, human