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By Emily Massengale, Biochemistry
Advisor: Ruxandra Dima
Presentation ID: PM_D04
Abstract: Microtubules (MTs) are intracellular biopolymers of tubulin dimers made up of alpha and beta tubulin. These microtubules along with MT associated proteins (MAPs) regulate various cellular functions such intracellular transport, cell division, etc. Among these MAPs are microtubule severing enzymes which belong to ATP-dependent homo-hexamerases of ATPases associated with various cellular activities (AAA+) family of enzymes. These severing enzymes bind to the acidic residue rich carboxy terminal tails (CTTs) of the tubulin dimers in different orientations, but the exact mechanism of binding and severing is unknown. We used molecular docking studies to investigate the initial binding and different interactions responsible for binding of the CTTs to various regions of the severing enzyme and identify the role of these isoforms of CTTs in microtubule severing. We identified that beta preferably binds to pore loop regions, whereas alpha binds to nucleotide binding domain region.