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    CHCHD4 coiled-coil-helix-coiled-coil-helix domain containing 4 [ Homo sapiens (human) ]

    Gene ID: 131474, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    CHCHD4 regulates the expression of mitochondrial genes that are essential for tumour cell growth.

    CHCHD4 regulates the expression of mitochondrial genes that are essential for tumour cell growth.
    Thomas LW, Stephen JM, Ashcroft M.

    08/22/2024
    [The glutathionylation of the human mitochondrial protein MIA40 regulates ROS homeostasis].

    [The glutathionylation of the human mitochondrial protein MIA40 regulates ROS homeostasis].
    Arab R, Sitolle J, Ziga J, Golinelli-Cohen MP.

    02/28/2024
    Impaired AIF-CHCHD4 interaction and mitochondrial calcium overload contribute to auditory neuropathy spectrum disorder in patient-iPSC-derived neurons with AIFM1 variant.

    Impaired AIF-CHCHD4 interaction and mitochondrial calcium overload contribute to auditory neuropathy spectrum disorder in patient-iPSC-derived neurons with AIFM1 variant.
    Qiu Y, Wang H, Fan M, Pan H, Guan J, Jiang Y, Jia Z, Wu K, Zhou H, Zhuang Q, Lei Z, Ding X, Cai H, Dong Y, Yan L, Lin A, Fu Y, Zhang D, Yan Q, Wang Q., Free PMC Article

    07/3/2023
    CHCHD4 (MIA40) and the mitochondrial disulfide relay system.

    CHCHD4 (MIA40) and the mitochondrial disulfide relay system.
    Al-Habib H, Ashcroft M., Free PMC Article

    01/29/2022
    AIF meets the CHCHD4/Mia40-dependent mitochondrial import pathway.

    AIF meets the CHCHD4/Mia40-dependent mitochondrial import pathway.
    Reinhardt C, Arena G, Nedara K, Edwards R, Brenner C, Tokatlidis K, Modjtahedi N.

    10/24/2020
    First group to discover the expression of the human CHCHD4 isoforms and first to call the human gene CHCHD4, and to clone and show the expression of its alternatively expressed CHCHD4 isoforms (CHCHD4.1 and CHCHD4.2).

    Human CHCHD4 mitochondrial proteins regulate cellular oxygen consumption rate and metabolism and provide a critical role in hypoxia signaling and tumor progression.
    Yang J, Staples O, Thomas LW, Briston T, Robson M, Poon E, Simões ML, El-Emir E, Buffa FM, Ahmed A, Annear NP, Shukla D, Pedley BR, Maxwell PH, Harris AL, Ashcroft M., Free PMC Article

    04/19/2017
    Compared to wild type control littermates, mice with a knockout of CHCHD4 exhibit reduced weight gain when fed a high-fat diet.

    Metabolic epistasis among apoptosis-inducing factor and the mitochondrial import factor CHCHD4.
    Modjtahedi N, Hangen E, Gonin P, Kroemer G., Free PMC Article

    06/28/2016
    Data show that the redox state of cytochrome c oxidase assembly protein 17 (Cox17), mitochondrial membrane transport protein Mia40 and superoxide dismutase 1 (SOD1) in the cytoplasm were directly observed with in-cell NMR spectroscopy.

    Direct structural evidence of protein redox regulation obtained by in-cell NMR.
    Mercatelli E, Barbieri L, Luchinat E, Banci L.

    05/28/2016
    our findings suggest that MIA40 reduction contributes to the effects of AIF deficiency on OXPHOS, as it may impact on the correct assembly and maintenance of the respiratory subunits.

    Loss of apoptosis-inducing factor critically affects MIA40 function.
    Meyer K, Buettner S, Ghezzi D, Zeviani M, Bano D, Nicotera P., Free PMC Article

    05/14/2016
    results demonstrate an indispensable role for hMIA40 for the export of Fe-S clusters from mitochondria.

    Human mitochondrial MIA40 (CHCHD4) is a component of the Fe-S cluster export machinery.
    Murari A, Thiriveedi VR, Mohammad F, Vengaldas V, Gorla M, Tammineni P, Krishnamoorthy T, Sepuri NB.

    01/2/2016
    Data indicate that poptosis-inducing factor (AIF) controls the mitochondrial import of mitochondrial membrane transport protein CHCHD4.

    Interaction between AIF and CHCHD4 Regulates Respiratory Chain Biogenesis.
    Hangen E, Féraud O, Lachkar S, Mou H, Doti N, Fimia GM, Lam NV, Zhu C, Godin I, Muller K, Chatzi A, Nuebel E, Ciccosanti F, Flamant S, Bénit P, Perfettini JL, Sauvat A, Bennaceur-Griscelli A, Ser-Le Roux K, Gonin P, Tokatlidis K, Rustin P, Piacentini M, Ruvo M, Blomgren K, Kroemer G, Modjtahedi N.

    09/26/2015
    In aggregate these data suggest that the Mia40/lfALR system has a broad sequence specificity and that potential substrates may be protected from adventitious oxidation by kinetic sequestration within the mitochondrial IMS.

    Mia40 is a facile oxidant of unfolded reduced proteins but shows minimal isomerase activity.
    Hudson DA, Thorpe C., Free PMC Article

    09/26/2015
    Import and oxidative folding of proteins are kinetically and functionally coupled and depend on the expression of Mia40, ALR, and the intracellular glutathione pool.

    Protein import and oxidative folding in the mitochondrial intermembrane space of intact mammalian cells.
    Fischer M, Horn S, Belkacemi A, Kojer K, Petrungaro C, Habich M, Ali M, Küttner V, Bien M, Kauff F, Dengjel J, Herrmann JM, Riemer J., Free PMC Article

    02/8/2014
    Data indicate that decreased CHCHD4 expression prevents the mitochondrial translocation of p53 while augmenting its nuclear localization and activity.

    Mitochondrial disulfide relay mediates translocation of p53 and partitions its subcellular activity.
    Zhuang J, Wang PY, Huang X, Chen X, Kang JG, Hwang PM., Free PMC Article

    01/4/2014
    illustrate a very atypical behaviour for the Mia40 precursor compared to other substrates of the MIA pathway. By contrast, interaction with Erv1 occurs after 5 min of import and relies on a more stringent specificity

    Biogenesis of yeast Mia40 - uncoupling folding from import and atypical recognition features.
    Chatzi A, Sideris DP, Katrakili N, Pozidis C, Tokatlidis K.

    11/23/2013
    mitochondrial localization of MIA40 requires sulfhydryl oxidase ALR in heterologous expression yeast system.

    Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial biogenesis of human MIA40.
    Sztolsztener ME, Brewinska A, Guiard B, Chacinska A.

    07/27/2013
    Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR.

    Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR.
    Banci L, Bertini I, Calderone V, Cefaro C, Ciofi-Baffoni S, Gallo A, Kallergi E, Lionaki E, Pozidis C, Tokatlidis K., Free PMC Article

    05/28/2011
    Observational study of gene-disease association. (HuGE Navigator)

    Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
    Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL, O'Brien SJ., Free PMC Article

    12/5/2010
    Catalysis involves a flow of reducing equivalents from the reduced CxC cysteine motif of Mia40 to distal and then proximal CxxC motifs of long-form ALR to the flavin ring and, finally, to cytochrome c or molecular oxygen.

    Augmenter of liver regeneration: substrate specificity of a flavin-dependent oxidoreductase from the mitochondrial intermembrane space.
    Daithankar VN, Farrell SR, Thorpe C., Free PMC Article

    01/21/2010
    analysis of how mitochondrial biogenesis switches the sorting pathway of the intermembrane space receptor Mia40

    Mitochondrial biogenesis, switching the sorting pathway of the intermembrane space receptor Mia40.
    Chacinska A, Guiard B, Müller JM, Schulze-Specking A, Gabriel K, Kutik S, Pfanner N., Free PMC Article

    01/21/2010
    After passage across the translocase of the mitochondrial outer membrane Erv1 interacts via disulfide bonds with Mia40.

    The sulfhydryl oxidase Erv1 is a substrate of the Mia40-dependent protein translocation pathway.
    Terziyska N, Grumbt B, Bien M, Neupert W, Herrmann JM, Hell K.

    01/21/2010
    biogenesis and function of MIA40 in the mitochondrial intermembrane space is dependent on redox processes involving conserved cysteine residues

    Functional and mutational characterization of human MIA40 acting during import into the mitochondrial intermembrane space.
    Hofmann S, Rothbauer U, Mühlenbein N, Baiker K, Hell K, Bauer MF.

    01/21/2010
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