Persistent Link:
http://hdl.handle.net/10150/579057
Title:
The Role of dMiro in the Distribution and Health of Mitochondria
Author:
Sangston, Ryan Michael
Issue Date:
2015
Publisher:
The University of Arizona.
Rights:
Copyright © 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.
Abstract:
In neurons, regions of high energy demand, like synapses, can be far away from the cell body. Therefore, neurons require efficient mitochondrial transport for maintaining synaptic function and preventing degeneration. Miro is a protein that has been found to be necessary for proper distribution of mitochondria into axons and dendrites of neurons. Miro has an N-terminal GTPase domain (G1), a C-terminal GTPase domain (G2), two calcium-binding EF-hand domains, a variable domain of unknown function, and a transmembrane domain that anchors the protein to the outer mitochondrial membrane. This project examines two main questions concerning the role of Drosophila Miro (dMiro) for mitochondrial transport. First, it examines whether the potentially constitutively active mutations A20V in the G1 domain and K455V in the G2 domain of dMiro affect kinetics of mitochondrial transport. Second, it examines the potential role of the variable domain of dMiro for mitochondrial transport, function, and morphology. I found that the A20V mutation in the G1 domain had no significant effects on the kinetics of mitochondrial transport, even though loss-of-function mutations of the domain abolished the distribution of mitochondria into axons and dendrites. Furthermore, the K455V in the G2 domain had no effect on transport, and did not modulate the function of the G1 domain. Finally, I found that the variable domain of dMiro confers different functional characteristics to the three different isoforms of dMiro. Specifically, I found that the medium dMiro isoform interacts differently with the mitochondrial fusion protein Marf.
Type:
text; Electronic Thesis
Degree Name:
B.S.
Degree Level:
bachelors
Degree Program:
Honors College; Neuroscience and Cognitive Science
Degree Grantor:
University of Arizona
Advisor:
Zinsmaier, Konrad

Full metadata record

DC FieldValue Language
dc.language.isoen_USen
dc.titleThe Role of dMiro in the Distribution and Health of Mitochondriaen_US
dc.creatorSangston, Ryan Michaelen
dc.contributor.authorSangston, Ryan Michaelen
dc.date.issued2015en
dc.publisherThe University of Arizona.en
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
dc.description.abstractIn neurons, regions of high energy demand, like synapses, can be far away from the cell body. Therefore, neurons require efficient mitochondrial transport for maintaining synaptic function and preventing degeneration. Miro is a protein that has been found to be necessary for proper distribution of mitochondria into axons and dendrites of neurons. Miro has an N-terminal GTPase domain (G1), a C-terminal GTPase domain (G2), two calcium-binding EF-hand domains, a variable domain of unknown function, and a transmembrane domain that anchors the protein to the outer mitochondrial membrane. This project examines two main questions concerning the role of Drosophila Miro (dMiro) for mitochondrial transport. First, it examines whether the potentially constitutively active mutations A20V in the G1 domain and K455V in the G2 domain of dMiro affect kinetics of mitochondrial transport. Second, it examines the potential role of the variable domain of dMiro for mitochondrial transport, function, and morphology. I found that the A20V mutation in the G1 domain had no significant effects on the kinetics of mitochondrial transport, even though loss-of-function mutations of the domain abolished the distribution of mitochondria into axons and dendrites. Furthermore, the K455V in the G2 domain had no effect on transport, and did not modulate the function of the G1 domain. Finally, I found that the variable domain of dMiro confers different functional characteristics to the three different isoforms of dMiro. Specifically, I found that the medium dMiro isoform interacts differently with the mitochondrial fusion protein Marf.en
dc.typetexten
dc.typeElectronic Thesisen
thesis.degree.nameB.S.en
thesis.degree.levelbachelorsen
thesis.degree.disciplineHonors Collegeen
thesis.degree.disciplineNeuroscience and Cognitive Scienceen
thesis.degree.grantorUniversity of Arizonaen
dc.contributor.advisorZinsmaier, Konraden
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