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Showing 1–26 of 26 results
Advanced filters: Author: David J Pagliarini Clear advanced filters

  • The mitochondrial phosphatase PPTC7 has previously been linked to the maintenance of mitochondrial content, but the mechanisms underlying this phenotype remain unclear. Here, the authors demonstrate that loss of Pptc7 results in metabolic defects and further suggest that PPTC7 is a regulator of receptor-mediated mitophagy.

    • Natalie M. Niemi
    • Lia R. Serrano
    • David J. Pagliarini
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-17

  • Coenzyme Q (CoQ) is a lipid made in the inner mitochondrial membrane with antioxidant roles throughout the cell, but regulation of its cellular distribution is unclear. Here the authors identify two proteins that have reciprocal CoQ trafficking functions to help coordinate CoQ localization in yeast.

    • Zachary A. Kemmerer
    • Kyle P. Robinson
    • David J. Pagliarini
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-11

  • Baker et al. show that mitochondrial stress recovery requires mobilization of lipid droplet triacylglycerol stores to facilitate cardiolipin biosynthesis and mitochondrial biogenesis.

    • Zakery N. Baker
    • Yunyun Zhu
    • David J. Pagliarini
    ResearchOpen Access
    Nature Cell Biology
    Volume: 27, P: 298-308

  • Mito-SEPs are small peptides that can modulate oxidative metabolism in mitochondria. Here the authors show that C15ORF48 encodes a mito-SEP, MOCCI, capable of altering mitochondria respiration to suppress inflammation, while C15ORF48 3’ untranslated region also contains a miRNA, miR-147b, that synergizes with MOCCI to modulate host anti-viral responses.

    • Cheryl Q. E. Lee
    • Baptiste Kerouanton
    • Lena Ho
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-22

  • Rashan, Bartlett and colleagues show that mammalian 4-hydroxy fatty acids are primarily catabolized by ACAD10 and ACAD11 (atypical mitochondrial and peroxisomal acyl-CoA dehydrogenases, respectively) that use phosphorylation in their reaction mechanisms.

    • Edrees H. Rashan
    • Abigail K. Bartlett
    • David J. Pagliarini
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 1622-1632

  • Sung et al. provide a powerful pipeline based on deep mutational scanning to elucidate the molecular mechanisms of mitochondrial complex I assembly and predict pathogenicity of mutations in complex I assembly factors.

    • Andrew Y. Sung
    • Rachel M. Guerra
    • David J. Pagliarini
    Research
    Nature Metabolism
    Volume: 6, P: 1128-1142

  • Tai et al. show that Hem25p—a mitochondrial glycine transporter required for haem biosynthesis—is also needed for isopentenyl pyrophosphate (IPP) transport into mitochondria and coenzyme Q synthesis in Saccharomyces cerevisiae.

    • Jonathan Tai
    • Rachel M. Guerra
    • David J. Pagliarini
    Research
    Nature Cell Biology
    Volume: 25, P: 1616-1624

  • Murray et al. identified and characterized a small-molecule inhibitor of human COQ8A, which belongs to the UbiB protein family and is essential for coenzyme Q biosynthesis.

    • Nathan H. Murray
    • Christopher R. M. Asquith
    • David J. Pagliarini
    Research
    Nature Chemical Biology
    Volume: 19, P: 230-238

  • The mitochondria houses several phosphatases, but their function is not well characterized. Here, the authors show that mitochondrial phosphatase Pptc7 is important during development for proper mitochondrial function and has a role regulating protein import with the translocase subunit Timm50.

    • Natalie M. Niemi
    • Gary M. Wilson
    • David J. Pagliarini
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-14

  • Protein phosphorylation plays critical roles in myriad cell processes. In this work, the authors apply new mass spectrometer technology to detect and quantify tens of thousands of protein phosphorylation sites within one hour or less of analysis. This technology has potential to greatly accelerate biological discovery.

    • Noah M. Lancaster
    • Pavel Sinitcyn
    • Joshua J. Coon
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-18

  • Direct infusion–shotgun proteome analysis (DI-SPA) using data-independent acquisition mass spectrometry (DIA-MS) achieves fast and reproducible results by omitting the liquid-chromatography fractionation step and directly performing gas-phase peptide fractionation by ion mobility.

    • Jesse G. Meyer
    • Natalie M. Niemi
    • Joshua J. Coon
    Research
    Nature Methods
    Volume: 17, P: 1222-1228

  • Defining subcellular locations and interacting partners for proteins accelerates their functional characterization. A new in vivo tagging approach achieves both for mitochondrial matrix proteins and helps connect a key oxidoreductase to coenzyme Q biosynthesis.

    • Rachel M. Guerra
    • David J. Pagliarini
    News & Views
    Nature Chemical Biology
    Volume: 20, P: 132-133

  • Reactive nitrogen species can cause profound inhibition of α-ketoacid dehydrogenase complexes via covalent S-modifications of the E2 subunit’s catalytic lipoic arm. The enzymes’ substrate, CoA, can mediate targeted delivery of such modifications.

    • Gretchen L. Seim
    • Steven V. John
    • Jing Fan
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 19, P: 265-274

  • Macrophages engage in a sequence of dynamic functional changes during immune responses. Here the authors elucidate a two-stage remodelling of the tricarboxylic acid cycle during this process, which is driven by regulation of the pyruvate dehydrogenase and the oxoglutarate dehydrogenase complexes, and causes transient accumulation of immunoregulatory metabolites.

    • Gretchen L. Seim
    • Emily C. Britt
    • Jing Fan
    Research
    Nature Metabolism
    Volume: 1, P: 731-742

  • Systematic metabolite profiling across cancer cell lines uncovers patterns associated with genetic and epigenetic features and reveals dysregulated metabolic states that can be exploited for anticancer therapy

    • Haoxin Li
    • Shaoyang Ning
    • William R. Sellers
    Research
    Nature Medicine
    Volume: 25, P: 850-860

  • The mitochondrial proteome is highly complex, comprising ~1,000–1,500 proteins in mammals. Recent technological advances are now helping to refine the mitochondrial proteome and are assisting in characterizing mitochondrial protein functions, paving the way for better diagnosis and treatment of mitochondrial diseases.

    • Zakery N. Baker
    • Patrick Forny
    • David J. Pagliarini
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 25, P: 65-82