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You keep me hangin' on

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Date Issued:
2012
Summary:
Dynactin is a multisubunit protein complex that functions as a processivity cofactor to cytoplasmic dynein, assisting in vesicle transport and cell division. Independent of dynein,dynactin also serves to anchor microtubules to the centrosome. The functions of the majority of dynactin's subunits have been described to a certain degree ; however, the p24 subunit remains largely uncharacterized. Among the few things that are known about p24 are that it has a predicted molecular weight of about 20,822 Da, forms an a-helix, and binds directly to the p150[Glued] subunit. In order to explore its function further, we have performed shRNA-mediated knockdown, and fluorescent microscopy. We observe that microtubule disorganization is amplified due to the loss of p24. Our findings support the model that p24 serves as reinforcement to stabilize p150[Glued] at the centrosome.
Title: You keep me hangin' on: dynactin's p24 is essential for microtube anchoring.
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Name(s): Le, Ariel.
Harriet L. Wilkes Honors College
Type of Resource: text
Genre: Thesis
Issuance: multipart monograph
Date Issued: 2012
Publisher: Florida Atlantic University
Physical Form: electronic
electronic resource
Extent: vii, 34 p. : ill. (some col.)
Language(s): English
Summary: Dynactin is a multisubunit protein complex that functions as a processivity cofactor to cytoplasmic dynein, assisting in vesicle transport and cell division. Independent of dynein,dynactin also serves to anchor microtubules to the centrosome. The functions of the majority of dynactin's subunits have been described to a certain degree ; however, the p24 subunit remains largely uncharacterized. Among the few things that are known about p24 are that it has a predicted molecular weight of about 20,822 Da, forms an a-helix, and binds directly to the p150[Glued] subunit. In order to explore its function further, we have performed shRNA-mediated knockdown, and fluorescent microscopy. We observe that microtubule disorganization is amplified due to the loss of p24. Our findings support the model that p24 serves as reinforcement to stabilize p150[Glued] at the centrosome.
Identifier: 819325818 (oclc), 3355592 (digitool), FADT3355592 (IID), fau:1418 (fedora)
Note(s): by Ariel Le.
Thesis (B.A.)--Florida Atlantic University, Honors College, 2012.
Includes bibliography.
Electronic reproduction. Boca Raton, Fla., 2012. Mode of access: World Wide Web.
Subject(s): Cytoskeletal proteins
Cell organellles -- Formation
Microtubules
Molecular biology
Held by: FBoU FAUER
Persistent Link to This Record: http://purl.flvc.org/FAU/3355592
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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