Cellular effects of knocking down expression of dynactin's p150Glued subunit

Dynactin is made up of 11 different peptide units with a distinct ultrastructure consisting of a shoulder/sidearm complex and a rod-like domain. It functions as a cofactor for cytoplasmic dynein, assisting in the processes of long-range vesicle movements, microtubule anchoring, endomembrane localization, and mitotic progression. Previous studies have shown that dynactin binds to microtubules at the centrosome, keeping a radial arrangement during interphase. The p150Glued subunit contains two distinct microtubule-binding domains: CAP-Gly and Basic. While both of these sequences can interact with microtubules, CAP-Gly has a much greater affinity for binding to microtubules, suggesting that the two domains may be active for different functions within the cell. Using shRNA, I looked at the overexpression and knockdown of p150Glued and examined the effect that had on the cell. Knockdown has been shown to cause defects in centrosome organization and mitotic index.