FAK interaction with MBD2: A link from cell adhesion to nuclear chromatin remodeling?

Cell Adhesion & Migration
Lin Mei, Wen-Cheng Xiong

Abstract

Cell adhesion, migration, proliferation and differentiation are tightly linked and coordinated cellular processes. Cell adhesion dependent gene expression is believed to contribute to such coordination. Focal adhesion kinase (FAK) and its related protein, PYK2 (proline rich tyrosine kinase 2), are a major family of cell adhesion activated tyrosine kinases that play important roles in these cellular processes. Whereas FAK or PYK2 is known to be a scaffold protein, recruiting many cytoplasmic proteins into the focal adhesion complex and regulating focal adhesion turnover and cell migration, how FAK or PYK2 links to the nuclei and regulates gene expression remain largely unclear. We recently report a new signaling of FAK in regulating heterochromatin remodeling by its interaction with MBD2 (Methyl CpG binding domain protein 2), which may underlie FAK regulation of myogenin expression and muscle differentiation. Two insights have been obtained through the analysis of FAK-MBD2 interaction. The interaction appears to be sufficient, but not necessary, for FAK translocation into or maintaining in the nucleus. The nuclear FAK-MBD2 complexes cause altered heterochromatin organization and decreased MBD2 association with HDAC1 (histone dea...Continue Reading

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Citations

May 21, 2013·Molecules and Cells·Ssang-Taek Steve Lim
Apr 10, 2014·Cell Adhesion & Migration·Maaike C W van den Berg, Boudewijn M T Burgering
May 2, 2014·Frontiers in Cellular Neuroscience·Kristin DerligRegina Dahlhaus
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Jul 12, 2011·Microvascular Research·Noureddine ZebdaKonstantin G Birukov

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