Date of Award


Document Type

Union College Only

Degree Name

Bachelor of Science



First Advisor

Barbara Donowski




microtubule, enzyme, tubulin, stability


Recently, studies have linked microtubule (MT) behavior and the activity of the enzyme, AMPK (adenosine monophosphate-activated protein kinase), known as the master regulator of cell metabolism. AMPK is activated when glucose or other cellular energy sources are depleted. Also cellular stress, i.e. ATP (adenosine triphosphate) depletion, causes MTs to become hyperstable. Since post-translational modifications (PTMs), i.e. acetylation and detyrosination, are known to increase the stability of MTs, we studied the relationship between AMPK and the acetylation and detyrosination of hyper-stable MTs. We investigated whether MTs in ATPdepleted C3H10T1/2 mouse fibroblasts are heavily acetylated and detyrosinated, and if so,whether these PTMs are dependent on AMPK activity. When cells were depleted of ATP via treatment with sodium azide and 2-deoxyglucose, there was a significant increase in hyper-stable MTs with these PTMs, as seen by western blot and immunofluorescence. ATP-depletion also led to an increase in the active form of AMPK, phosphorylated-AMPK. To observe if there was a relationship between AMPK activation and these PTMs of MTs, we used an AMPK inhibitor, Compound C (CC), in the presence of ATP depletion to determine if the inhibition of AMPK leads to a decrease in these PTMs of hyper-stable MTs. Through western blot, we observed that the inhibition of AMPK had no significant effect on the PTMs of hyper-stable MTs. However, CC did not reduce AMPK to control levels, so we still believe there is a connection between AMPK activity and these PTMs, but other methods need to be used to lower AMPK levels.