Mutational and functional analyses of the dynein heavy chain indicate the existence of an apical-sistal transport cycle in cells

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Mutational and functional analyses of the dynein heavy chain indicate the existence of an apical-sistal transport cycle in cells

Please use this identifier to cite or link to this item: http://hdl.handle.net/10355/13110

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dc.contributor.advisor King, Stephen J. (Stephen James) en
dc.contributor.author Sivagurunathan, Senthilkumar
dc.date.accessioned 2012-03-02T16:00:32Z
dc.date.available 2012-03-02T16:00:32Z
dc.date.issued 2012-03-02
dc.date.submitted 2011 Fall en
dc.identifier.uri http://hdl.handle.net/10355/13110
dc.description Title from PDF of title page, viewed on March 2, 2012 en
dc.description Dissertation advisor: Stephen J. King en
dc.description Vita en
dc.description Includes bibliographic references (p. 163-187) en
dc.description Thesis (Ph.D.)--School of Biological Sciences. University of Missouri--Kansas City, 2011 en
dc.description.abstract The organization, survival, and function of eukaryotic cells depend on intracellular transport governed by the microtubule based molecular motors cytoplasmic dynein and kinesin. Dynein carries out the inward transport of cargos whereas kinesins are responsible for the outward movement. Although intracellular transport is necessary for the function of all cells, polarized cells in particular have specific transport needs due to their asymmetry and elongated shape. These extraordinary requirements necessitate efficient long range microtubule based transport mechanisms. The anterograde transport needs in these cells are satisfied by a variety of kinesins but only a single cytoplasmic dynein fulfills the retrograde transport requirements. Dynein is a megadalton, multiprotein motor complex composed of heavy chains, intermediate chains, light intermediate chains, and light chains. The heavy chains form the force producing motor entity of the dynein complex and the rest of the components are involved in linking dynein to cargoes. The heavy chain has the two functional domains; motor head and a tail. The motor head is responsible for the ATP hydrolysis as well as the microtubule interaction of the dynein complex. The tail domain is involved in the homodimerization of heavy chains as well as interaction with the other dynein subunits. The enormous size and complex mechanochemisty of dynein has complicated our understanding of the functions and regulation of dynein. The study presented here utilized the ascomycete fungus Neurospora crassa in a series of genetic, cell biological and complementing biochemical approaches to study dynein function and regulation. The study is divided into two sections of which the first section will focus on the effects of spontaneous dynein heavy chain mutations on dynein functions in the hyphae of Neurospora crassa along with biochemical analyses of purified dynein from wildtype and a representative mutant strain. The second section focuses on the effect of a mouse neurodegenerative dynein heavy chain mutation on N. crassa dynein function both in vivo and in vitro. The aim of this work is to understand the structure-function relationship and the regulation of dynein. en_US
dc.description.tableofcontents Introduction -- Materials and methods -- Characterization of dynein heavy chain mutations in n. crassa -- Analyses of a mouse neurodegenerative dhc mutation in neurospora crassa -- Conclusions en
dc.format.extent xx, 188 pages en
dc.language.iso en_US en_US
dc.publisher University of Missouri--Kansas City en
dc.subject.lcsh Dynein en
dc.subject.lcsh Neurospora crassa en
dc.subject.other Dissertation -- University of Missouri--Kansas City -- Biology en
dc.title Mutational and functional analyses of the dynein heavy chain indicate the existence of an apical-sistal transport cycle in cells en_US
dc.type Thesis en_US
thesis.degree.discipline Molecular Biology and Biochemistry and Cell Biology and Biophysics en
thesis.degree.grantor University of Missouri--Kansas City en
thesis.degree.name Ph.D. en
thesis.degree.level Doctoral en


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