{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/86758"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/86758","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Signals Regulating Organelle Transport in Melanophores","abstract":"To investigate the mechanisms of regulation of motor proteins driving melanosome transport, the phosphorylation states of the motors and the levels of motors on the organelles were examined. Immunoprecipitation of myosin V showed that the motor subunit is more heavily phosphorylated in cells aggregating pigment compared to cells dispersing pigment. Furthermore, levels of myosin V on melanosomes are higher in cells dispersing pigment. Therefore the association of myosin V with melanosomes correlates with its dephosphorylation. Immunoprecipitation of cytoplasmic dynein showed that proteins at the molecular weights of the light intermediate chains are differentially phosphorylated in aggregated and dispersed cells. Both motor subunits of kinesin II are phosphorylated in melanophores, but were not observed to be differentially phosphorylated. The levels of kinesin II and dynein on aggregating or dispersing melanosomes remain constant.","abstract_html":"To investigate the mechanisms of regulation of motor proteins driving melanosome transport, the phosphorylation states of the motors and the levels of motors on the organelles were examined. Immunoprecipitation of myosin V showed that the motor subunit is more heavily phosphorylated in cells aggregating pigment compared to cells dispersing pigment. Furthermore, levels of myosin V on melanosomes are higher in cells dispersing pigment. Therefore the association of myosin V with melanosomes correlates with its dephosphorylation. Immunoprecipitation of cytoplasmic dynein showed that proteins at the molecular weights of the light intermediate chains are differentially phosphorylated in aggregated and dispersed cells. Both motor subunits of kinesin II are phosphorylated in melanophores, but were not observed to be differentially phosphorylated. The levels of kinesin II and dynein on aggregating or dispersing melanosomes remain constant.","abstract_has_math":false,"creators":["Reilein, Amy Ruth"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Vladimir I. 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Immunoprecipitation of myosin V showed that the motor subunit is more heavily phosphorylated in cells aggregating pigment compared to cells dispersing pigment. Furthermore, levels of myosin V on melanosomes are higher in cells dispersing pigment. Therefore the association of myosin V with melanosomes correlates with its dephosphorylation. Immunoprecipitation of cytoplasmic dynein showed that proteins at the molecular weights of the light intermediate chains are differentially phosphorylated in aggregated and dispersed cells. Both motor subunits of kinesin II are phosphorylated in melanophores, but were not observed to be differentially phosphorylated. The levels of kinesin II and dynein on aggregating or dispersing melanosomes remain constant.","Made available in DSpace on 2015-09-28T15:17:52Z (GMT). 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Immunoprecipitation of myosin V showed that the motor subunit is more heavily phosphorylated in cells aggregating pigment compared to cells dispersing pigment. Furthermore, levels of myosin V on melanosomes are higher in cells dispersing pigment. Therefore the association of myosin V with melanosomes correlates with its dephosphorylation. Immunoprecipitation of cytoplasmic dynein showed that proteins at the molecular weights of the light intermediate chains are differentially phosphorylated in aggregated and dispersed cells. Both motor subunits of kinesin II are phosphorylated in melanophores, but were not observed to be differentially phosphorylated. The levels of kinesin II and dynein on aggregating or dispersing melanosomes remain constant.","Made available in DSpace on 2015-09-28T15:17:52Z (GMT). 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