Sandbox Reserved 1788: Difference between revisions

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'''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.
'''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.


[[Image:LPA_in_membrane4.fw.png|200px|center|thumb|'''Figure 1:''' LPA receptor (blue) bound to the cell membrane. The binding pocket is highlighted in red. The added bRIL protein is highlighted in orange.]] 




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