Researcher:
Mutlu, Nebibe

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Master Student

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Nebibe

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Mutlu

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Mutlu, Nebibe

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20143

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Researcher Of Publications: search.filters.isAuthorOfPublication.2e1e0257-1ded-4840-a45a-84b33d688599

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    Nutrient-sensing signaling pathways determine the outcome of mitochondrial dysfunction
    (Wiley-Blackwell, 2014) Department of Molecular Biology and Genetics; N/A; N/A; N/A; N/A; Dunn, Cory David; Garipler, Görkem; Mutlu, Nebibe; Lack, Nathan Alan; Other; Master Student; Master Student; Faculty Member; Department of Molecular Biology and Genetics; College of Sciences; Graduate School of Sciences and Engineering; Graduate School of Sciences and Engineering; School of Medicine; N/A; N/A; N/A; 120842
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    PublicationOpen Access
    Activation of the pleiotropic drug resistance pathway can promote mitochondrial DNA retention by fusion-defective mitochondria in saccharomyces cerevisiae
    (Genetics Society America (GSA), 2014) Department of Chemical and Biological Engineering; Dunn, Cory David; Mutlu, Nebibe; Garipler, Görkem; Akdoğan, Emel; Faculty Member; Department of Chemical and Biological Engineering; College of Sciences
    Genetic and microscopic approaches using Saccharomyces cerevisiae have identified many proteins that play a role in mitochondrial dynamics, but it is possible that other proteins and pathways that play a role in mitochondrial division and fusion remain to be discovered. Mutants lacking mitochondrial fusion are characterized by rapid loss of mitochondrial DNA. We took advantage of a petite-negative mutant that is unable to survive mitochondrial DNA loss to select for mutations that allow cells with fusion-deficient mitochondria to maintain the mitochondrial genome on fermentable medium. Nextgeneration sequencing revealed that all identified suppressor mutations not associated with known mitochondrial division components were localized to PDR1 or PDR3, which encode transcription factors promoting drug resistance. Further studies revealed that at least one, if not all, of these suppressor mutations dominantly increases resistance to known substrates of the pleiotropic drug resistance pathway. Interestingly, hyperactivation of this pathway did not significantly affect mitochondrial shape, suggesting that mitochondrial division was not greatly affected. Our results reveal an intriguing genetic connection between pleiotropic drug resistance and mitochondrial dynamics.
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    PublicationOpen Access
    Deletion of conserved protein phosphatases reverses defects associated with mitochondrial DNA damage in Saccharomyces cerevisiae
    (National Academy of Sciences, 2014) Department of Molecular Biology and Genetics; Garipler, Görkem; Mutlu, Nebibe; Lack, Nathan Alan; Dunn, Cory David; Faculty Member; Faculty Member; Department of Molecular Biology and Genetics; School of Medicine; Graduate School of Sciences and Engineering; N/A; N/A; 120842; N/A
    Mitochondrial biogenesis is regulated by signaling pathways sensitive to extracellular conditions and to the internal environment of the cell. Therefore, treatments for disease caused by mutation of mtDNA may emerge from studies of how signal transduction pathways command mitochondrial function. We have examined the role of phosphatases under the control of the conserved alpha 4/Tap42 protein in cells lacking a mitochondrial genome. We found that deletion of protein phosphatase 2A (PP2A) or of protein phosphatase 6 (PP6) protects cells from the reduced proliferation, mitochondrial protein import defects, lower mitochondrial electrochemical potential, and nuclear transcriptional response associated with mtDNA damage. Moreover, PP2A or PP6 deletion allows viability of a sensitized yeast strain after mtDNA loss. Interestingly, the Saccharomyces cerevisiae ortholog of the mammalian AMP-activated protein kinase was required for the full benefits of PP6 deletion and also for proliferation of otherwise wild-type cells lacking mtDNA. Our work highlights the important role that nutrient-responsive signaling pathways can play in determining the response to mitochondrial dysfunction.