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Cytokinesis in Drosophila melanogaster.
~
Farkas, Rebecca Michal.
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Cytokinesis in Drosophila melanogaster.
Record Type:
Language materials, printed : Monograph/item
Title/Author:
Cytokinesis in Drosophila melanogaster./
Author:
Farkas, Rebecca Michal.
Description:
152 p.
Notes:
Adviser: Margaret T. Fuller.
Contained By:
Dissertation Abstracts International63-01B.
Subject:
Biology, Cell. -
Online resource:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3038088
ISBN:
0493517456
Cytokinesis in Drosophila melanogaster.
Farkas, Rebecca Michal.
Cytokinesis in Drosophila melanogaster.
- 152 p.
Adviser: Margaret T. Fuller.
Thesis (Ph.D.)--Stanford University, 2002.
Cytokinesis, the process by which a dividing cell partitions its contents, is essential for development and reproduction. In animal cells, cytokinesis occurs by the deepening of a furrow in the plasma membrane. Furrow ingression is driven by the constriction of an underlying actomyosin ring. The mechanisms by which cells regulate and mediate the localization, assembly, constriction, and disassembly of the actomyosin ring are poorly understood. It is also not clear what additional changes must occur within the cell to allow cleavage furrow ingression.
ISBN: 0493517456Subjects--Topical Terms:
1017686
Biology, Cell.
Cytokinesis in Drosophila melanogaster.
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152 p.
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Adviser: Margaret T. Fuller.
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Source: Dissertation Abstracts International, Volume: 63-01, Section: B, page: 0030.
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Thesis (Ph.D.)--Stanford University, 2002.
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Cytokinesis, the process by which a dividing cell partitions its contents, is essential for development and reproduction. In animal cells, cytokinesis occurs by the deepening of a furrow in the plasma membrane. Furrow ingression is driven by the constriction of an underlying actomyosin ring. The mechanisms by which cells regulate and mediate the localization, assembly, constriction, and disassembly of the actomyosin ring are poorly understood. It is also not clear what additional changes must occur within the cell to allow cleavage furrow ingression.
520
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I took a genetic approach to identify components and regulators of the cytokinesis machinery in <italic>Drosophila</italic> spermatocytes. In a large-scale screen, I identified mutations that disrupted cytokinesis and assigned them to fifty complementation groups. Based on cytological characterization of mutants with strong phenotypes, I assigned seventeen genes to different functional groups. The cytological data indicated that cytokinesis occurs in discrete steps with different genes acting at different points in the pathway. Six of the genes identified in the screen were required for spermatid elongation as well as for cytokinesis, suggesting that similar mechanisms may drive the two processes. To begin to characterize these common mechanisms, I cloned one of the genes, <italic>four way stop</italic> (<italic>fws</italic>). Cytological analysis indicated that functional Fws is required for cleavage furrow ingression during spermatocyte meiotic divisions. The Fws protein was homologous to human GTC90 and yeast Cod4p, proteins required for vesicle fusion <italic>in vitro </italic> and <italic>in vivo</italic>, respectively. Fws protein localized to the Golgi apparatus and was required for Golgi membrane fusion in <italic> Drosophila</italic> spermatids, suggesting that Fws may promote vesicle transport through the Golgi. Cytokinesis and polarized cell growth both may require Fws-mediated vesicle transport for the delivery of new membrane and/or Golgi-modified cargo to expanding regions of the cell surface. Preliminary results suggested that at least two other genes required for both furrow ingression and spermatid elongation, <italic>onion rings</italic> and <italic>funnel cakes </italic>, also encode vesicle transport proteins. One of the other genes required for both cytokinesis and spermatid elongation was necessary for actin disassembly, suggesting that the two processes may require similar pathways for actin reorganization.
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School code: 0212.
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Stanford University.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3038088
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