The Effect Of Myotonic Dystrophy Kinase Related Cdc42...

Introduction/Background: Cell motility is heavily studied, mainly due to the importance of cell motility in a living cell for normal physiological functions. 3-Phosphoinositide-dependent kinase 1 (PDK1) is integral kinase that phosphorylates serine/threonine residues in activation loops of various proteins that function in metabolism, grown, proliferation, and survival of various cells (Fyffe et al., 2013). Located on the human chromosome 16p13.3, it is ubiquitously expressed in human tissue, as well as other animals such as Drosophilla (Alessi et al., 1997). But PDK1 functionality is beyond just normal human cells, and has been heavily studied in directional cell migration for both physiological and pathological processes such as wound healing and tumor metastasis (Gagliardi et al., 2014). Myotonic dystrophy kinase-related CDC42-binding kinase ÃŽ ± (MRCKÃŽ ±) is a Rho-binding kinase that has been shown to cause actin cytoskeleton reorganization for cell motility through light-chain phosphorylation, which is required in cell motility (Chen et al., 1999). MRCK kinases play integral roles in actin-myosin regulations by being downstream effectors of GTPase-CDC42. Activation of GTPase-CDC42 and actin cytoskeleton reorganizations are both vital in cell motility, as the conversion of GTP to GDP provide actin filament degradation, which in turn allows for the formation of new filaments needed for movement of the cell. The authors of this paper attempt to deduce which domains of PDK1