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FAK and PAX-illin get involved in leukocyte diapedesis

Francis W Luscinskas1

  • 1Center for Excellence in Vascular Biology, Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA. fluscinskas@partners.org

European Journal of Immunology
|January 24, 2012
PubMed

Insights

Researchers identified focal adhesion proteins, paxillin and focal adhesion kinase (FAK), as new regulators of neutrophil diapedesis. This finding implicates FAK and paxillin in crucial steps of leukocyte recruitment, expanding our understanding of immune cell migration.

Area of Science:

  • Immunology
  • Cell Biology

Background:

  • Leukocyte recruitment involves complex interactions between endothelial cells, adhesion molecules, and chemokines.
  • Recent research highlights the importance of endothelial cell-to-matrix adhesion in regulating leukocyte migration.

Purpose of the Study:

  • To identify novel regulators of neutrophil diapedesis (transendothelial migration).
  • To investigate the role of focal adhesion proteins in leukocyte recruitment.

Main Methods:

  • The study by Parsons et al. identified paxillin and focal adhesion kinase (FAK) as key players.
  • The commentary discusses the implications of these findings for understanding leukocyte adhesion cascade.

Main Results:

  • Paxillin and FAK are implicated in the regulation of neutrophil diapedesis.
  • These focal adhesion proteins play roles in both proximal (leukocyte rolling) and distal (diapedesis) stages of leukocyte recruitment.

Conclusions:

  • Focal adhesion kinase (FAK) and paxillin are newly identified regulators of neutrophil transendothelial migration.
  • Understanding the role of these proteins enhances knowledge of the multistep adhesion cascade in leukocyte recruitment.

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