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Synthesis and biological evaluation of novel analogues of dictyostatin
Title
Synthesis and biological evaluation of novel analogues of dictyostatin.
Creator
Paterson, Ian, Gardner, Nicola M., Poullennec, Karine G., Wright, Amy E.
Date Issued
2007
PURL
http://purl.flvc.org/FCLA/DT/2763290
Subject Headings
Microtubules --Research--Methodology, Microtubules
Format
Document (PDF)
Synthetic Analogues of the Microtubule-Stabilizing Agent (+)-Discodermolide: Preparation and Biological Activity
Title
Synthetic Analogues of the Microtubule-Stabilizing Agent (+)-Discodermolide: Preparation and Biological Activity.
Creator
Gunasekera, Sarath P., Mickel, Stuart J., Daeffler, Robert, Niederer, Daniel, Wright, Amy E., Linley, P. A., Pitts, Tara P.
Date Issued
2004
PURL
http://purl.flvc.org/FCLA/DT/3164107
Subject Headings
Microtubules, Cancer --Research, Biopharmaceutics, Molecular biology, Stereochemistry
Format
Document (PDF)
Total synthesis of a library of designed hybrids of the microtubule-stabilising anticancer agents taxol, discodermolide and dictyostatin
Title
Total synthesis of a library of designed hybrids of the microtubule-stabilising anticancer agents taxol, discodermolide and dictyostatin.
Creator
Paterson, Ian, Naylor, G. J., Fujita, T., Guzman, Esther A., Wright, Amy E.
Date Issued
2010
PURL
http://purl.flvc.org/fau/fd/FA00007065
Subject Headings
Antineoplastic agents, Paclitaxel, Polyketides, Microtubules, Tubulin Modulators, Marine natural products
Format
Document (PDF)
Stereochemical determination of dictyostatin, a novel microtubule-stabilising macrolide from the marine sponge Corallistidae sp.
Title
Stereochemical determination of dictyostatin, a novel microtubule-stabilising macrolide from the marine sponge Corallistidae sp.
Creator
Paterson, Ian, Britton, R., Delgado, Oscar, Wright, Amy E.
Date Issued
2004
PURL
http://purl.flvc.org/fau/fd/FA00007061
Subject Headings
Macrolides, Sponges, Tubulin Modulators, Stereochemistry, Microtubules, Polyketides, Antimitotic Agents
Format
Document (PDF)
Characterization of the kinesin KlF9 in mammalian cell cycle progression
Title
Characterization of the kinesin KlF9 in mammalian cell cycle progression.
Creator
Hoke, Jordan, Rivera, Miguel A., Billow, Alexa M., Alsina, Laura, Quintyne, Nicholas
Date Issued
2012-04-06
PURL
http://purl.flvc.org/fcla/dt/3352239
Subject Headings
KIF9 protein, Microtubules, Cell cycle progression, Cell division, Kinesin
Format
Document (PDF)
Knockdown of dynactin's p150[Glued] subunit abrogates microtubule organization
Title
Knockdown of dynactin's p150[Glued] subunit abrogates microtubule organization.
Creator
Roeckner, Jared Todd., Harriet L. Wilkes Honors College
Abstract/Description
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...
Show moreDynactin 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.
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Date Issued
2009
PURL
http://purl.flvc.org/FAU/209998
Subject Headings
Cytoskeletal proteins, Cell organelles, Formation, Microtubules, Molecular biology
Format
Document (PDF)
Contributions of dynactin's p150[Glued] subunit's binding domains to microtubule anchoring at the centrosome
Title
Contributions of dynactin's p150[Glued] subunit's binding domains to microtubule anchoring at the centrosome.
Creator
Schneider, Rebecca., Harriet L. Wilkes Honors College
Abstract/Description
Intracellular transport carries out very important roles within the cell including mitosis, organization, and organelle function. In order for effective transport using the motor protein dynein, a cofactor named dynactin is required. Of dynactin's many subunits, p150[Glued] holds the most responsibility for effective microtubule organization throughout the cell and the necessary anchoring at the centrosome. P150[Glued] holds two areas of high binding potential, the CAP-Gly region and the...
Show moreIntracellular transport carries out very important roles within the cell including mitosis, organization, and organelle function. In order for effective transport using the motor protein dynein, a cofactor named dynactin is required. Of dynactin's many subunits, p150[Glued] holds the most responsibility for effective microtubule organization throughout the cell and the necessary anchoring at the centrosome. P150[Glued] holds two areas of high binding potential, the CAP-Gly region and the Basic region. Each of these binding domains have different binding potentials and affinities for microtubules. The CAP-Gly region binds tightly the microtubules for a longer period of tiem ; the Basic region binds loosely to microtubules. Throughout the course of my research, I manipulated these two regions binding affinity for microtubules and evaluated the resulting cells ability to effectively organize microtubules and anchor them properly at the centrosome.
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Date Issued
2012
PURL
http://purl.flvc.org/FAU/3359326
Subject Headings
Cytoskeletal proteins, Microtubules, Centrosomes, Cell organelles, Formation, Molecular biology, Tubulins
Format
Document (PDF)
Dynactin is a processivity factor for dynein in vivo
Title
Dynactin is a processivity factor for dynein in vivo.
Creator
Fulton, Edward., Harriet L. Wilkes Honors College
Abstract/Description
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...
Show moreDynein 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.
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Date Issued
2009
PURL
http://purl.flvc.org/FAU/209990
Subject Headings
Cell organelles, Formation, Microtubules, Cytoskeletal proteins, Molecular biology
Format
Document (PDF)
Differential functionality of microtubule binding motifs in the p150[Glued] subunit of dynactin
Title
Differential functionality of microtubule binding motifs in the p150[Glued] subunit of dynactin.
Creator
Mallen, Michael Luis., Harriet L. Wilkes Honors College
Abstract/Description
Dynactin is a multi-subunit protein complex that is the required cofactor for the cytoplasmic motor protein, dynein. Dynactin is critical for cytoplasmic activities such as vesicle transport, cytoskeletal organization, membrane organization and mitotic progression as it serves to increase processivity of dynein. The main subunit in focus for this study is the sidearm extension p150Glued. On the exposed end (N-terminus) lie two different microtubule binding motifs: CAP-Gly and Basic. CAP-Gly...
Show moreDynactin is a multi-subunit protein complex that is the required cofactor for the cytoplasmic motor protein, dynein. Dynactin is critical for cytoplasmic activities such as vesicle transport, cytoskeletal organization, membrane organization and mitotic progression as it serves to increase processivity of dynein. The main subunit in focus for this study is the sidearm extension p150Glued. On the exposed end (N-terminus) lie two different microtubule binding motifs: CAP-Gly and Basic. CAP-Gly has a high binding affinity for microtubules, while Basic binds the microtubules quite weakly. It is at this location that dynactin is proposed to assist in the processivity of transporting cargo long distances in the cell, by providing additional support for the dynein molecule as it progresses along the microtubule. Analysis of the effects of overexpression of these motifs, alone or in tandem, suggested that there was no disruption of the dynein/dynactin interaction, but its ability to act in a processive manner had been perturbed. Effects on non-dynamic processes, such as Golgi localization and microtubule organization were generally weak, but effects were greater on y-tubulin organization. While this could suggest a defect in centrosome organization, we propose that it instead shows that cargo motility in the affected cells is defective, and that transport of centrosomal proteins to the centrosome is interrupted, suggesting a broader cargo-transport defect may be evident in these cells.
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Date Issued
2007
PURL
http://purl.flvc.org/FAU/11613
Subject Headings
Cytoskeletal proteins, Tubulins, Microtubules, Centrosomes, Cell organelles, Formation
Format
Document (PDF)
You keep me hangin' on
Title
You keep me hangin' on: dynactin's p24 is essential for microtube anchoring.
Creator
Le, Ariel., Harriet L. Wilkes Honors College
Abstract/Description
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...
Show moreDynactin 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.
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Date Issued
2012
PURL
http://purl.flvc.org/FAU/3355592
Subject Headings
Cytoskeletal proteins, Cell organellles, Formation, Microtubules, Molecular biology
Format
Document (PDF)
Centrosome recruitment
Title
Centrosome recruitment: analysis of protein changes during S phase.
Creator
Raborn, Erik., Harriet L. Wilkes Honors College
Abstract/Description
The centrosome is a dynamic and highly active organelle within the cell. It plays a pivotal role in mitosis driving several of the physical changes that are taking place. The centrosome self-replicates before mitosis in order to set up two spindle poles on opposite sides of the cell. This leads to the creation of a mother and daughter centrosomes within a cell that have distinct components. This project will examine the recruitment of proteins to the centrosome as a cell progresses through...
Show moreThe centrosome is a dynamic and highly active organelle within the cell. It plays a pivotal role in mitosis driving several of the physical changes that are taking place. The centrosome self-replicates before mitosis in order to set up two spindle poles on opposite sides of the cell. This leads to the creation of a mother and daughter centrosomes within a cell that have distinct components. This project will examine the recruitment of proteins to the centrosome as a cell progresses through the cell cycle. The proteins examined are (Sd(B-tubulin, (Sf(B-tubulin, Nek 2, Centrin2, p150Glued, EB-1, and dynein intermediate chain. In addition, chromosome arrangement was determined. By examining these proteins we hope to establish a logical order for the interactions of these proteins and their key contributions to cell cycle progression and completion, specifically dealing with the development of the mother and daughter centrosomes.
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Date Issued
2009
PURL
http://purl.flvc.org/FAU/3325085
Subject Headings
Cell organelles, Formation, Cytoskeletal proteins, Cell division, Tubulins, Microtubules
Format
Document (PDF)