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Anchors aweigh: using shRNA TO MAP p150Glued functionality in anchoring microtubules at the centrosome

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Date Issued:
2013
Summary:
Dynactin is a multisubunit protein complex required for proper functioning of the microtubule motor, cytoplasmic dynein. Dynactin serves as a processivity factor for the motor as well as a cargo adaptor, allowing dynein to function in a wide array of cellular processes. Additionally, dynactin serves as a microtubule anchor. The p150Glued subunit of dynactin is of particular importance to these processes, as it possesses dynactin’s microtubule binding sequences, termed the CAP-Gly and Basic domains. These domains have differential affinities for microtubules, with CAP-Gly binding to microtubules with a higher affinity than Basic. By testing a set of shRNA plasmids with antisense sequences to the untranslated region of p150Glued we have found effective knockdown of the protein in COS-7 cells; future researchers can then introduce plasmids for p150Glued lacking either the CAP-Gly or Basic domains, or both, potentially showing a differential effect on anchoring, dependent upon which domain is present.
Title: Anchors aweigh: using shRNA TO MAP p150Glued functionality in anchoring microtubules at the centrosome.
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Name(s): Hazellief, Kristal
Quintyne, Nicholas
Harriet L. Wilkes Honors College
Type of Resource: text
Genre: Thesis
Date Created: 2013
Date Issued: 2013
Publisher: Florida Atlantic University
Place of Publication: Boca Raton, Florida
Physical Form: pdf
Extent: 32 p.
Language(s): English
Summary: Dynactin is a multisubunit protein complex required for proper functioning of the microtubule motor, cytoplasmic dynein. Dynactin serves as a processivity factor for the motor as well as a cargo adaptor, allowing dynein to function in a wide array of cellular processes. Additionally, dynactin serves as a microtubule anchor. The p150Glued subunit of dynactin is of particular importance to these processes, as it possesses dynactin’s microtubule binding sequences, termed the CAP-Gly and Basic domains. These domains have differential affinities for microtubules, with CAP-Gly binding to microtubules with a higher affinity than Basic. By testing a set of shRNA plasmids with antisense sequences to the untranslated region of p150Glued we have found effective knockdown of the protein in COS-7 cells; future researchers can then introduce plasmids for p150Glued lacking either the CAP-Gly or Basic domains, or both, potentially showing a differential effect on anchoring, dependent upon which domain is present.
Identifier: FA00003516 (IID)
Note(s): Includes bibliography.
Thesis (B.A.)--Florida Atlantic University, Harriet L. Wilkes Honors College, 2013.
Held by: Florida Atlantic University Libraries
Sublocation: FAU Digital Library
Persistent Link to This Record: http://purl.flvc.org/fau/fd/FA00003516
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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