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dc.contributor.advisorZinsmaier, Konrad
dc.contributor.authorKuhn, Terra Melody
dc.creatorKuhn, Terra Melodyen_US
dc.date.accessioned2013-08-09T16:16:21Z
dc.date.available2013-08-09T16:16:21Z
dc.date.issued2013
dc.identifier.citationKuhn, Terra Melody. (2013). Effects of Dmiro Isoforms on Mitochondrial Transport, Health, and Morphology (Bachelor's thesis, University of Arizona, Tucson, USA).
dc.identifier.urihttp://hdl.handle.net/10150/297683
dc.description.abstractMicrotubule (MT)-based transport of mitochondria into dendrites and axons is vital for sustaining neuronal excitation and synaptic function. The mitochondrial GTPase Miro is critical for mitochondrial transport by linking MT motor proteins to mitochondria. In flies and mammals, Miro proteins contain a variable domain whose position but not sequence is highly conserved. In Drosophila, the shortest (Miro-S) and longest (Miro-L) isoform differ by only 21 amino acids while the medium isoform (Miro-M) is 8 amino acids shorter than Miro-L. To test the functional significance of these isoforms, we expressed each individually in miro null or wild type Drosophila neurons and found differential effects on mitochondrial transport, structure and health. Expression of Miro-L and -S fail to rescue the larval lethality of miro null mutants while Miro-M does. OE of Miro-L and -S but not -M is also lethal. The effects on viability correlate with effects on mitochondria. Miro-L and Miro-S primarily cause morphological changes of axonal mitochondria, and are less efficient in facilitating aspects of mitochondrial transport than Miro-M. In conclusion, our data suggest different roles and/or activities for each of the 3 Miro protein isoforms.
dc.language.isoenen_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/
dc.titleEffects of Dmiro Isoforms on Mitochondrial Transport, Health, and Morphologyen_US
dc.typetexten_US
dc.typeElectronic Thesisen_US
thesis.degree.grantorUniversity of Arizonaen_US
thesis.degree.levelbachelorsen_US
thesis.degree.disciplineHonors Collegeen_US
thesis.degree.disciplineMolecular and Cellular Biologyen_US
thesis.degree.nameB.S.en_US
refterms.dateFOA2018-08-30T09:49:15Z
html.description.abstractMicrotubule (MT)-based transport of mitochondria into dendrites and axons is vital for sustaining neuronal excitation and synaptic function. The mitochondrial GTPase Miro is critical for mitochondrial transport by linking MT motor proteins to mitochondria. In flies and mammals, Miro proteins contain a variable domain whose position but not sequence is highly conserved. In Drosophila, the shortest (Miro-S) and longest (Miro-L) isoform differ by only 21 amino acids while the medium isoform (Miro-M) is 8 amino acids shorter than Miro-L. To test the functional significance of these isoforms, we expressed each individually in miro null or wild type Drosophila neurons and found differential effects on mitochondrial transport, structure and health. Expression of Miro-L and -S fail to rescue the larval lethality of miro null mutants while Miro-M does. OE of Miro-L and -S but not -M is also lethal. The effects on viability correlate with effects on mitochondria. Miro-L and Miro-S primarily cause morphological changes of axonal mitochondria, and are less efficient in facilitating aspects of mitochondrial transport than Miro-M. In conclusion, our data suggest different roles and/or activities for each of the 3 Miro protein isoforms.


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