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Knockdown of dynactin's p150[Glued] subunit abrogates microtubule organization

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Date Issued:
2009
Summary:
Dynactin is a multifunctional protein complex composed of at least 11 different subunits. Dynactin functions as a cofactor for cytoplasmic dynein facilitating long-range vesicle movements, microtubule anchoring, endomembrane localization, and mitotic progression. Previous studies have shown that dynactin binds to microtubules at the centrosome maintaining a radial array in interphase. The p150Glued subunit contains two distinct microtubule-binding sequences named CAP-Gly and Basic. While both domains can interact with microtubule, CAP-Gly has a much greater affinity for binding to microtubules, suggesting that the two domains may be active for different dynactin-based functions within the cell. Using siRNA, we found that knockdown of p150Glued was sufficient to alter the maintenance of radial microtubule arrays, cause an increase in centrosome number and mitotic index. In the future we will replace the endogenous protein with versions lacking the CAP-Gly or Basic domains to investigate the contribution of each to microtubule anchoring and cytoskeletal architecture.
Title: Knockdown of dynactin's p150[Glued] subunit abrogates microtubule organization.
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Name(s): Roeckner, Jared Todd.
Harriet L. Wilkes Honors College
Type of Resource: text
Genre: Thesis
Issuance: multipart monograph
Date Issued: 2009
Publisher: Florida Atlantic University
Physical Form: electronic resource
Extent: vi, 25 p. : ill. (some col.)
Language(s): English
Summary: Dynactin is a multifunctional protein complex composed of at least 11 different subunits. Dynactin functions as a cofactor for cytoplasmic dynein facilitating long-range vesicle movements, microtubule anchoring, endomembrane localization, and mitotic progression. Previous studies have shown that dynactin binds to microtubules at the centrosome maintaining a radial array in interphase. The p150Glued subunit contains two distinct microtubule-binding sequences named CAP-Gly and Basic. While both domains can interact with microtubule, CAP-Gly has a much greater affinity for binding to microtubules, suggesting that the two domains may be active for different dynactin-based functions within the cell. Using siRNA, we found that knockdown of p150Glued was sufficient to alter the maintenance of radial microtubule arrays, cause an increase in centrosome number and mitotic index. In the future we will replace the endogenous protein with versions lacking the CAP-Gly or Basic domains to investigate the contribution of each to microtubule anchoring and cytoskeletal architecture.
Identifier: 781626627 (oclc), 209998 (digitool), FADT209998 (IID), fau:1372 (fedora)
Note(s): by Jared Todd Roeckner.
Thesis (B.A.)--Florida Atlantic University, Honors College, 2009.
Includes bibliography.
Electronic reproduction. Boca Raton, Fla., 2009. Mode of access: World Wide Web.
Subject(s): Cytoskeletal proteins
Cell organelles -- Formation
Microtubules
Molecular biology
Held by: FBoU FAUER
Persistent Link to This Record: http://purl.flvc.org/FAU/209998
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

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