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Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
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Structural basis for the interaction between focal adhesion kinase and CD4.

Marie-Line Garron1, James Arthos, Jean-François Guichou

  • 1INSERM, UMR554, 34090 Montpellier, France.

Journal of Molecular Biology
|December 15, 2007
PubMed
Summary

Focal adhesion kinase (FAK) binds to CD4 in T cells, forming a complex that influences cellular signaling during HIV infection. This interaction may offer an alternative signaling pathway and is disrupted by HIV-1 Nef.

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Assessment of the Synaptic Interface of Primary Human T Cells from Peripheral Blood and Lymphoid Tissue
06:27

Assessment of the Synaptic Interface of Primary Human T Cells from Peripheral Blood and Lymphoid Tissue

Published on: July 30, 2018

Area of Science:

  • Cellular Biology
  • Immunology
  • Virology

Background:

  • Focal adhesion kinase (FAK) is crucial for integrin signaling.
  • CD4 plays a key role in immune defense and T cell activation.
  • Both FAK and CD4 are involved in T cell signaling pathways, particularly during HIV infection.

Purpose of the Study:

  • To investigate the interaction between FAK and CD4 in T lymphocytes.
  • To elucidate the structural and functional consequences of FAK-CD4 complex formation.
  • To understand the role of this complex in T cell signaling during HIV infection.

Main Methods:

  • Crystallography to determine the structure of the FAK-CD4 complex.
  • Microcalorimetry to assess the binding thermodynamics.
  • T cell stimulation assays using HIV-1 gp120 and antigen.
  • Analysis of protein-protein interactions in T cells.

Main Results:

  • The focal adhesion targeting (FAT) domain of FAK specifically binds to the CD4 endocytosis motif in vitro.
  • The FAK-CD4 complex is structurally and thermodynamically similar to FAK-paxillin complexes.
  • FAK binding to CD4 is mutually exclusive with Lck binding and is triggered by HIV-1 gp120 in T cells.
  • HIV-1 Nef may displace FAK from CD4 in infected cells.

Conclusions:

  • The FAK-CD4 complex provides an alternative signaling route in T cells.
  • This complex links gp120 engagement to distinct T cell signaling during HIV infection.
  • HIV-1 Nef might displace FAK from CD4 to promote T cell survival by preventing apoptosis.