Jul
01

Post #3: Done with RTH! Back to Oncogenesis

Hi everyone! I am very excited to share with you my results for my RTH experiments. So far, have not found a significant difference in N/C ratios between the wild-type receptor, and the mutant TRa1 receptors.

Figure 1 shows the images I obtained from the fluorescent microscope. As we can see, there is no difference in localization patterns; all of the variants were mostly localized to the cell’s nucleus.

 

Fig 1. Cells expressing wild type TR-a1, Mutant 1 and Mutant 2. The FITC channel represents the GFP-tagged receptor, while DAPI represents the cell's nuclei.

Fig 1. Cells expressing wild type TR-a1, Mutant 1 and Mutant 2. The FITC channel represents the GFP-tagged receptor, while DAPI represents the cell’s nuclei.

In the next couple of weeks, I will move away from RTH and go back to my research on TR oncogenesis. I will be working with receptor tc-TRa1 a mutant that was originally found in tissues of patients with thyroid cancer. This mutant has a residue substitution in the receptor’s NLS-2, and in my previous research in the Allison lab, it exhibited significant cytosolic distributions with a tendency to form protein aggregates (Figure 2).

Fig 2. Mutant tc-TR-a1. The blue represents DAPI-stained nuclei, and the green represents the GFP-tagged receptor.

Fig 2. Mutant tc-TR-a1. The blue represents DAPI-stained nuclei, and the green represents the GFP-tagged receptor.

 

My plan over the next couple weeks is to co-express this mutant receptor in HeLa cells, alongside a marker for protein aggregation. I will be using DNA expressing protein light chain 3 (LC3). LC3 is commonly found in sites of cell autophagy – a process that regulates the degradation of organelles and cellular debris. We hypothesize that if these protein aggregates are being degraded by the cell through autophagy, then we should see some overlap between our receptor and our light chain 3.

I can’t wait to share my results with you!

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