Sar1, a novel regulator of ER-mitochondrial contact sites

• Main Authors: Ackema K.B., Prescianotto-Baschong C., Hench J., Wang S.C., Chia Z.H., Mergentaler H., Bard F., Frank S., Spang A.
• Other Authors: BIOCHEMISTRY
• Format: Article
• Published: 2019
• Subjects: aspartic acid; dynamin; glycine; guanosine triphosphatase; mutant protein; regulator protein; Sar1 protein; unclassified drug; Caenorhabditis elegans protein; dynamin-related protein 1, C elegans; monomeric guanine nucleotide binding protein; Saccharomyces cerevisiae protein; Sar1 protein, C elegans; SAR1 protein, S cerevisiae; SAR1A protein, human; small interfering RNA; vesicular transport protein; amino terminal sequence; Article; binding site; cell fusion; controlled study; endoplasmic reticulum; endoplasmic reticulum membrane; enzyme activation; enzyme activity; enzyme regulation; interphase; membrane structure; mitochondrial dynamics; mitochondrial membrane; mitochondrion; nonhuman; phenotype; protein depletion; regulatory mechanism; Saccharomyces cerevisiae; sar1D32G gene; amino acid substitution; animal; antagonists and inhibitors; Caenorhabditis elegans; chemistry; conserved sequence; gene expression regulation; genetics; HeLa cell line; human; intracellular membrane; ion transport; lipid metabolism; metabolism; mutation; signal transduction; ultrastructure; Amino Acid Substitution; Animals; Caenorhabditis elegans Proteins; Conserved Sequence; Dynamins; Endoplasmic Reticulum; Gene Expression Regulation; GTP Phosphohydrolases; HeLa Cells; Humans; Intracellular Membranes; Ion Transport; Lipid Metabolism; Mitochondria; Mitochondrial Dynamics; Monomeric GTP-Binding Proteins; Mutation; RNA, Small Interfering; Saccharomyces cerevisiae Proteins; Signal Transduction; Vesicular Transport Proteins
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/161576
• Institution: National University of Singapore

10.1371/journal.pone.0154280