Date of Award

2011

Document Type

Dissertation/Thesis

Submission Date

October 2026

Thesis/Dissertation Advisor [Chair]

Quintyne, Nicholas

Abstract

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.

Comments

Includes bibliography.

Extent

42 p.

Identifier

FA00003599

Download

Share

COinS