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  • PKC ε Phosphorylates and Mediates the Cell Membrane Localization of RhoA.

    ISRN Oncol. 2013:329063. doi: 10.1155/2013/329063. 2013. View on PubMed.
  • Authors

    Greg Cavey (Western Michigan University Homer Stryker M.D. School of Medicine), Gregory Cavey (Innovative Mass Spectrometry LLC), Su T, Straight S, Bao L, Xie X, Lehner CL, Teknos TN, and Pan Q
  • Abstract

    Protein kinase C ε (PKC ε ) signals through RhoA to modulate cell invasion and motility. In this study, the multifaceted interaction between PKC ε and RhoA was defined. Phosphopeptide mapping revealed that PKC ε phosphorylates RhoA at T127 and S188. Recombinant PKC ε bound to recombinant RhoA in the absence of ATP indicating that the association between PKC ε and RhoA does not require an active ATP-docked PKC ε conformation. Activation of PKC ε resulted in a dramatic coordinated translocation of PKC ε and RhoA from the cytoplasm to the cell membrane using time-lapse fluorescence microscopy. Stoichiometric FRET analysis revealed that the molecular interaction between PKC ε and RhoA is a biphasic event, an initial peak at the cytoplasm and a gradual prolonged increase at the cell membrane for the entire time-course (12.5 minutes). These results suggest that the PKC ε -RhoA complex is assembled in the cytoplasm and subsequently recruited to the cell membrane. Kinase inactive (K437R) PKC ε is able to recruit RhoA to the cell membrane indicating that the association between PKC ε and RhoA is proximal to the active catalytic site and perhaps independent of a PKC ε -RhoA phosphorylation event. This work demonstrates, for the first time, that PKC ε phosphorylates and modulates the cell membrane translocation of RhoA.

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