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  1. Article: ROG1 encodes a monoacylglycerol lipase in Saccharomyces cerevisiae

    Vishnu Varthini, Lakshmanaperumal / Kandasamy Selvaraju / Malathi Srinivasan / Vasanthi Nachiappan

    Federation of European Biochemical Societies FEBS letters. 2015 Jan. 02, v. 589, no. 1

    2015  

    Abstract: Lipid metabolism is extensively studied in Saccharomyces cerevisiae. Here, we report that revertant of glycogen synthase kinase mutation-1 (Rog1p) possesses monoacylglycerol (MAG) lipase activity in S. cerevisiae. The lipase activity of Rog1p was ... ...

    Abstract Lipid metabolism is extensively studied in Saccharomyces cerevisiae. Here, we report that revertant of glycogen synthase kinase mutation-1 (Rog1p) possesses monoacylglycerol (MAG) lipase activity in S. cerevisiae. The lipase activity of Rog1p was confirmed in two ways: through analysis of a strain with a double deletion of ROG1 and monoglyceride lipase YJU3 (yju3Δrog1Δ) and by site-directed mutagenesis of the ROG1 lipase motif (GXSXG). Rog1p is localized in both the cytosol and the nucleus. Overexpression of ROG1 in a ROG1-deficient strain resulted in an accumulation of reactive oxygen species. These results suggest that Rog1p is a MAG lipase that regulates lipid homeostasis.
    Keywords Saccharomyces cerevisiae ; acylglycerol lipase ; cytosol ; glycogen synthase kinases ; homeostasis ; lipid metabolism ; lipids ; reactive oxygen species ; site-directed mutagenesis
    Language English
    Dates of publication 2015-0102
    Size p. 23-30.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/j.febslet.2014.11.019
    Database NAL-Catalogue (AGRICOLA)

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  2. Article ; Online: APOE expression and secretion are modulated by mitochondrial dysfunction.

    Wynne, Meghan E / Ogunbona, Oluwaseun / Lane, Alicia R / Gokhale, Avanti / Zlatic, Stephanie A / Xu, Chongchong / Wen, Zhexing / Duong, Duc M / Rayaprolu, Sruti / Ivanova, Anna / Ortlund, Eric A / Dammer, Eric B / Seyfried, Nicholas T / Roberts, Blaine R / Crocker, Amanda / Shanbhag, Vinit / Petris, Michael / Senoo, Nanami / Kandasamy, Selvaraju /
    Claypool, Steven Michael / Barrientos, Antoni / Wingo, Aliza / Wingo, Thomas S / Rangaraju, Srikant / Levey, Allan I / Werner, Erica / Faundez, Victor

    eLife

    2023  Volume 12

    Abstract: Mitochondria influence cellular function through both cell-autonomous and non-cell autonomous mechanisms, such as production of paracrine and endocrine factors. Here, we demonstrate that mitochondrial regulation of the secretome is more extensive than ... ...

    Abstract Mitochondria influence cellular function through both cell-autonomous and non-cell autonomous mechanisms, such as production of paracrine and endocrine factors. Here, we demonstrate that mitochondrial regulation of the secretome is more extensive than previously appreciated, as both genetic and pharmacological disruption of the electron transport chain caused upregulation of the Alzheimer's disease risk factor apolipoprotein E (APOE) and other secretome components. Indirect disruption of the electron transport chain by gene editing of SLC25A mitochondrial membrane transporters as well as direct genetic and pharmacological disruption of either complexes I, III, or the copper-containing complex IV of the electron transport chain elicited upregulation of APOE transcript, protein, and secretion, up to 49-fold. These APOE phenotypes were robustly expressed in diverse cell types and iPSC-derived human astrocytes as part of an inflammatory gene expression program. Moreover, age- and genotype-dependent decline in brain levels of respiratory complex I preceded an increase in APOE in the 5xFAD mouse model. We propose that mitochondria act as novel upstream regulators of APOE-dependent cellular processes in health and disease.
    MeSH term(s) Animals ; Humans ; Mice ; Apolipoprotein E4/genetics ; Apolipoproteins E/genetics ; Apolipoproteins E/metabolism ; Astrocytes/metabolism ; Genotype ; Mitochondria/metabolism ; Mitochondria/pathology
    Chemical Substances Apolipoprotein E4 ; Apolipoproteins E
    Language English
    Publishing date 2023-05-12
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.85779
    Database MEDical Literature Analysis and Retrieval System OnLINE

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