Receptor-Mediated Endocytosis & Nuclear Signal Transduction


    According to the American Cancer Society, this year, about 569,490 Americans are expected to die of cancer, that’s more than 1,500 people a day. Based on my current research, I have may have found the link that may be triggering cell proliferation within the cell cycle. 

    Cells internalize molecules by the inward budding of plasma membrane vesicles through a process known as receptor-mediated endocytosis. My research focuses on these preliminary endocytic events, concentrating on the Rab5 protein. Activation of Rab5 is facilitated by a guanine nucleotide exchange factor (GEF) previously discovered called Rab5 activating protein 6 (also referred to as RAP6).     

    After completing biological techniques such as polymerase chain reaction, transformation, and transfection, I received the results I was seeking, which involved receiving a nuclear localization signal that links Rab5 to nuclear signal transduction. 

    The panel of results being displayed compares the full length (FL) RAP6 protein and its location in transfected 293T cells. Each construct features three images: GFP filtered images corresponding to the location of the RAP6 protein, the DAPI which stains the nucleus of all fixed cells, and the third column features the merged image of both GFP and DAPI staining. 

    It can be seen that RAP6 FL, Ras-GAP and Rab5GEF domains mainly localize in the cytosol of the cell whereas cells transfected with the Pleckstrin Homology (PH) domain alone, Rab5 localization was observed solely in the nucleus. Thus, these figures indirectly suggest that Rab5 may be linked to the patterns of localization that we observe. 

    Initial data suggests that cancer may be triggered by a nuclear localization signal in the PH domain of RAP6. All in all, my current research holds the potential cure for cancer and serves as a huge approach towards the biomedical sciences and humanity.

Receptor-Mediated Endocytosis and Nuclear Signal Transduction


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