SHOC2-PP1C-MRAS complex is a ternary holophosphatase complex formed by the individual proteins: SHOC2, PP1C, and MRAS. SHOC2-PP1C-MRAS complex is involved in cell proliferation because it functions as a regulator of RTK-RAS signaling by activating RAF through dephosphorization. Complex formation is initiated by ligand binding of receptor tyrosine kinase receptor(RTK). The RTK activates membrane bound MRAS by signaling the exchange of GDP for GTP. GTP bound MRAS initiates complex formation, this complex and is able to dephosphorylate the RAF complex leading to further downstream signaling effects.
Figure 3: Electrostatic illustration of the amphipathic binding pocket of the LPA1 receptor. This binding pocket was revealed by cutting away the exterior or the protein. This binding pocket, located in the interior of the protein, has both polar and nonpolar regions. The blue and red coloration highlight the positively and negatively charged regions, respectively, and the white color shows the nonpolar region of the binding pocket.
