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Integrative genomics identifies MC ... | Article | H1 Connect
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Mitochondria from diverse organisms are capable of transporting large amounts of Ca(2+) via a ruthenium-red-sensitive, membrane-potential-dependent mechani

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Keywords {🔍}

mcu, mitochondrial, protein, uniporter, calcium, finding, latest, recommendation, genomics, uptake, molecular, authors, channel, cookies, baughman, micu, membrane, cells, complex, essential, work, identify, mitochondria, mechanism, stefani, report, activity, biology, chemistry, proteomics, integrative, component, ccdca, based, genomic, transport, identity, function, findings, analysis, imm, hand, gene, data, cell, faculty, jun, show, physiological, relevant,

Topics {✒️}

art cell biology stimulating creb-mediated expression finding cryo-em structure increased ca2+ uptake drug target mitochondrial ca++ intake mitochondrial calcium uniporter bigger protein complex forty-kilodalton protein vivo rnai-based suppression mitochondrial ca2+ entry genome-wide profiling v5-tagged constructs fundamental step forward alter ca++ import creative bioinformatic approach finding evolutionary diversity finding dual functions isolated liver cells larger protein complex customize settings accept short intramembrane space human protein ccdc109a mitochondrial uniporter micu1 induce calcium transport small regulatory subunit finding proteolytic control integrative genomic databases integrative genomics major molecular component proper function mitochondrial membrane previous elegant work recently identified genetic manipulations ca2+ uptake mitochondrial uniporter faculty opinions calcium uptake authors identify e257 ca++ import disease & regeneration calcium uniporter finding structure liver morphology ca2+ transport transport ca2+ larger complex h1 company calcium entry

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ScholarlyArticle:
      context:https://schema.org
      headline:Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter.
      abstract:Mitochondria from diverse organisms are capable of transporting large amounts of Ca(2+) via a ruthenium-red-sensitive, membrane-potential-dependent mechanism called the uniporter. Although the uniporter's biophysical properties have been studied extensively, its molecular composition remains elusive. We recently used comparative proteomics to identify MICU1 (also known as CBARA1), an EF-hand-containing protein that serves as a putative regulator of the uniporter. Here, we use whole-genome phylogenetic profiling, genome-wide RNA co-expression analysis and organelle-wide protein coexpression analysis to predict proteins functionally related to MICU1. All three methods converge on a novel predicted transmembrane protein, CCDC109A, that we now call 'mitochondrial calcium uniporter' (MCU). MCU forms oligomers in the mitochondrial inner membrane, physically interacts with MICU1, and resides within a large molecular weight complex. Silencing MCU in cultured cells or in vivo in mouse liver severely abrogates mitochondrial Ca(2+) uptake, whereas mitochondrial respiration and membrane potential remain fully intact. MCU has two predicted transmembrane helices, which are separated by a highly conserved linker facing the intermembrane space. Acidic residues in this linker are required for its full activity. However, an S259A point mutation retains function but confers resistance to Ru360, the most potent inhibitor of the uniporter. Our genomic, physiological, biochemical and pharmacological data firmly establish MCU as an essential component of the mitochondrial Ca(2+) uniporter.
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WebPage:
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