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Commensal bacteria stimulate rapid phosphorylation of epithelial focal adhesion kinase that results in host cytoskeletal rearrangements
Author(s) -
Kumar Amrita,
Neish Andrew S.
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a766
Subject(s) - focal adhesion , microbiology and biotechnology , lactobacillus rhamnosus , cytoskeleton , phosphorylation , motility , biology , paxillin , tyrosine phosphorylation , ptk2 , cell adhesion , cell , probiotic , protein kinase a , bacteria , biochemistry , mitogen activated protein kinase kinase , genetics
The microflora residing in the lumen of the mammalian intestine exert significant effects on epithelial differentiation, barrier functions and reparative responses. However, the mechanism(s) by which bacteria modulate these processes remains poorly understood. Here we show that colonization of human epithelial cells in vitro with Lactobacillus rhamnosus GG stimulates rapid and reversible activation/phosphorylation of focal adhesion kinase (FAK), which results in increased cell adhesion, spreading and migration. FAK is a tyrosine kinase that functions as an important integrator of cell motility. We further show that butyrate, a microbial fermentation product of dietary fiber, also rapidly activates/phosphorylates FAK with similar downstream consequences. We conclude the normal gut flora and their products promote activation/phosphorylation of FAK, which influences changes in host cytoskeletal dynamics. These observations provide a mechanism that may explain the beneficial effects of live probiotic organisms employed as therapeutics. This research was supported by a Crohn’s and Colitis Foundation Research Grant.