Date of Award

2013

Document Type

Dissertation/Thesis

Submission Date

October 2026

Thesis/Dissertation Advisor [Chair]

Quintyne, Nicholas

Abstract

Dynactin, a multisubunit protein complex, serves as a processivity factor and cargo adaptor for the microtubule motor cytoplasmic dynein. Together, these proteins permit mitotic progression, intracellular trafficking, and endomembrane organization. Dynactin also independently anchors microtubules at the centrosome during interphase. In this study, we use shRNAs to knock down expression of the p24, p27, p62, and Arp1 subunits of dynactin to determine those components’ roles in anchoring. Recent work has shown p62’s importance to dynactin integrity (Yeh et al., 2012), and we confirm that its loss disrupts microtubule organization. The peripheral p27 and binding partner p25 seem to contribute to membrane selectivity and have little effect on dynactin structure and anchoring. We find that an intact dynactin complex is necessary to maintain microtubule organization via the anchoring complex. While not directly bound to microtubules, these subunits provide crucial structural support to facilitate interactions among dynactin and other centrosomal anchoring components.

Comments

Includes bibliography.

Extent

39 p.

Identifier

FA00003537

Share

COinS