title: FAK and PAX-illin get involved in leukocyte diapedesis.
abstract: A major focus of researchers studying leukocyte recruitment has been to identify and understand how cell surface endothelial adhesion molecules, cell-to-cell junctional protein complexes, secreted chemokines and chemoattractants, and the vessel basement membrane structure organization coordinate the process of leukocyte recruitment. As research expands beyond the components initially identified as being necessary for leukocyte recruitment, attention has turned to the structures that regulate endothelial cell-to-matrix adhesion. In this issue of the European Journal of Immunology, Parsons et al. [Eur. J. Immunol. 2012. 42: 436-446] identify new players in the regulation of neutrophil diapedesis (transendothelial migration), namely the focal adhesion proteins, paxillin and focal adhesion kinase (FAK). While understudied, and indeed previously underappreciated, in leukocyte diapedesis, this Commentary discusses how the work by Parsons et al. implicates FAK and paxillin in the proximal (leukocyte rolling) and distal (diapedesis) steps of the multistep adhesion cascade of leukocyte recruitment.
authors.affiliation: Center for Excellence in Vascular Biology, Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA. fluscinskas@partners.org
authors.forename: Francis W
authors.initials: FW
authors.lastname: Luscinskas
mesh_terms: D004727:Endothelium / Q000378:metabolism*; D051416:Focal Adhesion Protein-Tyrosine Kinases / Q000378:metabolism*; D006801:Humans; D009504:Neutrophils / Q000378:metabolism*; D051419:Paxillin / Q000378:metabolism*; D057705:Transendothelial and Transepithelial Migration / Q000276:immunology*
chemical_list: D051419:Paxillin; D051416:Focal Adhesion Protein-Tyrosine Kinases