@Article{mcb.2007.004.177,
AUTHOR = {Donald F. Ward Jr., William A. Williams, Nicole E. Schapiro, Samuel R. Christy, Genevieve L. Weber,  Megan Salt, Robert F. Klees, Adele Boskey, George E. Plopper ∗,‡},
TITLE = {Focal Adhesion Kinase Signaling Controls Cyclic Tensile Strain Enhanced Collagen I-Induced Osteogenic Differentiation of Human Mesenchymal Stem Cells},
JOURNAL = {Molecular \& Cellular Biomechanics},
VOLUME = {4},
YEAR = {2007},
NUMBER = {4},
PAGES = {177--188},
URL = {http://www.techscience.com/mcb/v4n4/28449},
ISSN = {1556-5300},
ABSTRACT = {Focal adhesion kinase (FAK) is a key integrator of integrin-mediated signals from the extracellular matrix to the cytoskeleton and downstream signaling molecules. FAK is activated by phosphorylation at specific tyrosine residues, which then stimulate downstream signaling including the ERK1/2 pathway, leading to a variety of cellular responses. In this study, we examined the effects of FAK point mutations at tyrosine residues (Y397, Y925, Y861, and Y576/7) on osteogenic differentiation of human mesenchymal stem cells exposed to collagen I and cyclic tensile strain. Our results demonstrate that FAK signaling emanating from Y397, Y925, and to a lesser extent Y576/7, but not from Y861, controls osteogenic differentiation through an ERK1/2 pathway, as measured by expression levels of key osteogenesis marker genes and subsequent matrix mineralization. These data indicate that FAK is a critical decision maker in extracellular matrix/strain-enhanced osteogenic differentiation.},
DOI = {10.3970/mcb.2007.004.177}
}