You are here

FAU Collections » FAU Research Repository » FAU College Collections » Harriet L. Wilkes Honors College » Honors Student Theses

Dynactin is a processivity factor for dynein in vivo

Download pdf | Full Screen View

Date Issued:
2009
Summary:
Dynein is a motor protein responsible for microtubule-based minus-end directed trafficking in eukaryotic cells. Dynactin is a protein complex involved in mitosis, embryonic development, intracellular trafficking and anchoring microtubules at the centrosome. While dynactin is widely recognized to improve the array of cargo with which dynein can associate, there has been some dispute over whether dynactin, which binds both dynein and microtubules, improves the distance that dynein can travel processively in the act of cargo trafficking before it dissociates from its microtubule. In this study, we compare movement parameters of wild type dynein-based vesicle movements with movements in cells where expression of dynactin's microtubule binding subunit, p150glued, has been knocked down. We find that dynactin does act as a processivity factor for dynein by increasing the distance that dynein can travel smoothly in a single movement event, but does not increase dynein's velocity.
Title: Dynactin is a processivity factor for dynein in vivo.
145 views
35 downloads
Name(s): Fulton, Edward.
Harriet L. Wilkes Honors College
Type of Resource: text
Genre: Thesis
Issuance: multipart monograph
Date Issued: 2009
Publisher: Florida Atlantic University
Physical Form: electronic
electronic resource
Extent: v, 28 leaves : ill. (some col.) ; 29 cm.
Language(s): English
Summary: Dynein is a motor protein responsible for microtubule-based minus-end directed trafficking in eukaryotic cells. Dynactin is a protein complex involved in mitosis, embryonic development, intracellular trafficking and anchoring microtubules at the centrosome. While dynactin is widely recognized to improve the array of cargo with which dynein can associate, there has been some dispute over whether dynactin, which binds both dynein and microtubules, improves the distance that dynein can travel processively in the act of cargo trafficking before it dissociates from its microtubule. In this study, we compare movement parameters of wild type dynein-based vesicle movements with movements in cells where expression of dynactin's microtubule binding subunit, p150glued, has been knocked down. We find that dynactin does act as a processivity factor for dynein by increasing the distance that dynein can travel smoothly in a single movement event, but does not increase dynein's velocity.
Identifier: 460176904 (oclc), 209990 (digitool), FADT209990 (IID), fau:1364 (fedora)
Note(s): by Edward Fulton.
Thesis (B.A.)--Florida Atlantic University, Honors College, 2009.
Bibliography: leaves 25-28.
Electronic reproduction. Boca Raton, Fla., 2009. Mode of access: World Wide Web.
Subject(s): Cell organelles -- Formation
Microtubules
Cytoskeletal proteins
Molecular biology
Held by: FBoU FAUER
Persistent Link to This Record: http://purl.flvc.org/FAU/209990
Use and Reproduction: Copyright © is held by the author, with permission granted to Florida Atlantic University to digitize, archive and distribute this item for non-profit research and educational purposes. Any reuse of this item in excess of fair use or other copyright exemptions requires permission of the copyright holder.
Host Institution: FAU

In Collections