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    UPS1 Ups1p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 850890, updated on 18-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Structural determinants of lipid specificity within Ups/PRELI lipid transfer proteins has been reported.

    Structural determinants of lipid specificity within Ups/PRELI lipid transfer proteins.
    Miliara X, Tatsuta T, Berry JL, Rouse SL, Solak K, Chorev DS, Wu D, Robinson CV, Matthews S, Langer T., Free PMC Article

    04/6/2019
    crystal structure of Ups1-Mdm35 bound with a phosphatidic acid (PA) molecule at 2.0 A resolution; study reveals molecular basis of Ups1-Mdm35-mediated PA binding and transfer and sheds new light on mechanism of intramitochondrial lipid transport by MSF1/PRELI family proteins

    Structural basis of intramitochondrial phosphatidic acid transport mediated by Ups1-Mdm35 complex.
    Yu F, He F, Yao H, Wang C, Wang J, Li J, Qi X, Xue H, Ding J, Zhang P., Free PMC Article

    04/23/2016
    The Ups1-Mdm35 complex constitutes a single domain that has a deep pocket and flexible Omega-loop lid. A basic residue at the pocket bottom and the Omega-loop lid are important for phosphatidic acid extraction from the membrane following Ups1 binding.

    Structural and mechanistic insights into phospholipid transfer by Ups1-Mdm35 in mitochondria.
    Watanabe Y, Tamura Y, Kawano S, Endo T., Free PMC Article

    04/16/2016
    PS is transferred from the mitochondrial outer membrane to the inner membrane independently of Psd1p, Ups1p, and Ups2p and decarboxylated to PE by Psd1p in the inner membrane

    Phosphatidylethanolamine biosynthesis in mitochondria: phosphatidylserine (PS) trafficking is independent of a PS decarboxylase and intermembrane space proteins UPS1P and UPS2P.
    Tamura Y, Onguka O, Itoh K, Endo T, Iijima M, Claypool SM, Sesaki H., Free PMC Article

    03/2/2013
    study identified Ups1 as a lipid transfer protein that can shuttle phosphatidic acid between mitochondrial membranes; lipid transfer required the dynamic assembly of Ups1 with Mdm35 and allowed conversion of phosphatidic acid to cardiolipin in the inner membrane

    Intramitochondrial transport of phosphatidic acid in yeast by a lipid transfer protein.
    Connerth M, Tatsuta T, Haag M, Klecker T, Westermann B, Langer T.

    12/8/2012
    Data suggest that Ups1p and Up2p proteins may function in phospholipid trafficking between the outer and inner mitochondrial membranes.

    Role for two conserved intermembrane space proteins, Ups1p and Ups2p, [corrected] in intra-mitochondrial phospholipid trafficking.
    Tamura Y, Onguka O, Hobbs AE, Jensen RE, Iijima M, Claypool SM, Sesaki H., Free PMC Article

    08/4/2012
    The authors show that Ups1, Ups2 and Ups3 protein import is mediated by another mitochondrial intermembrane space protein, Mdm35p.

    Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation.
    Tamura Y, Iijima M, Sesaki H., Free PMC Article

    10/4/2010
    The authors identified Mdm35, a member of the twin Cx9C protein family, as a novel interaction partner of Ups1 and Ups2.

    Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35.
    Potting C, Wilmes C, Engmann T, Osman C, Langer T., Free PMC Article

    10/4/2010
    Data report that two homologous intermembrane space proteins, Ups1p and Ups2p, control cardiolipin metabolism and affect the assembly state of TIM23 and its association with PAM in an opposing manner.

    Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria.
    Tamura Y, Endo T, Iijima M, Sesaki H., Free PMC Article

    01/21/2010
    deletion strains, ylr193cDelta/ylr193cDelta, yor305wDelta/yor305wDelta, and ypr170cDelta/ypr170cDelta, mate at very low frequencies with haploids of either or both MATa/MATalpha mating types.

    Single-gene deletions that restore mating competence to diploid yeast.
    Schmidlin T, Kaeberlein M, Kudlow BA, MacKay V, Lockshon D, Kennedy BK.

    01/21/2010
    The UPS1 protein is a novel mitochondrial protein required for the unique processing of Mgm1p and for normal mitochondrial shape.

    Ups1p, a conserved intermembrane space protein, regulates mitochondrial shape and alternative topogenesis of Mgm1p.
    Sesaki H, Dunn CD, Iijima M, Shepard KA, Yaffe MP, Machamer CE, Jensen RE., Free PMC Article

    01/21/2010
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