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. Author manuscript; available in PMC: 2012 Jun 1.
Published in final edited form as: IUBMB Life. 2011 Mar 24;63(6):390–396. doi: 10.1002/iub.447

Fig. 3.

Fig. 3

Cartoons of PAR-1-dependent signaling by APC and thrombin in endothelial cells when EPCR is either free or occupied by protein C. (Left Panel) EPCR interacts with caveolin-1 (Cav-1) within lipid-rafts of endothelial cells when it is not occupied by the Gla-domain of protein C. Thrombin cleavage of PAR-1 activates RhoA, up-regulates the NF-κB pathway and elicits disruptive signaling responses by signaling through G12/13 and/or Gq proteins. (Right Panel) The occupancy of EPCR by protein C leads to dissociation of EPCR from caveolin-1 and a switch in the specificity of PAR-1, presumably by signaling via the Gi-protein. Under these conditions, the thrombin cleavage of PAR-1 activates Rac1, inhibits the activation of the NF-κB pathway and initiates protective responses in endothelial cells. See the text for more detail. The figure is adopted from Ref. 39 with modifications.