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    MIEF2 mitochondrial elongation factor 2 [ Homo sapiens (human) ]

    Gene ID: 125170, updated on 19-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Fatty acyl-coenzyme A activates mitochondrial division through oligomerization of MiD49 and MiD51.

    Fatty acyl-coenzyme A activates mitochondrial division through oligomerization of MiD49 and MiD51.
    Liu A, Kage F, Abdulkareem AF, Aguirre-Huamani MP, Sapp G, Aydin H, Higgs HN.,

    08/14/2024
    MIEF2 reprograms lipid metabolism to drive progression of ovarian cancer through ROS/AKT/mTOR signaling pathway.

    MIEF2 reprograms lipid metabolism to drive progression of ovarian cancer through ROS/AKT/mTOR signaling pathway.
    Zhao S, Cheng L, Shi Y, Li J, Yun Q, Yang H., Free PMC Article

    10/2/2021
    MIEF2 over-expression promotes tumor growth and metastasis through reprogramming of glucose metabolism in ovarian cancer.

    MIEF2 over-expression promotes tumor growth and metastasis through reprogramming of glucose metabolism in ovarian cancer.
    Zhao S, Zhang X, Shi Y, Cheng L, Song T, Wu B, Li J, Yang H., Free PMC Article

    09/11/2021
    Mitochondrial fragmentation enables localized signaling required for cell repair.

    Mitochondrial fragmentation enables localized signaling required for cell repair.
    Horn A, Raavicharla S, Shah S, Cox D, Jaiswal JK., Free PMC Article

    02/20/2021
    An epigenetic increase in mitochondrial fission by MiD49 and MiD51 regulates the cell cycle in cancer: Diagnostic and therapeutic implications.

    An epigenetic increase in mitochondrial fission by MiD49 and MiD51 regulates the cell cycle in cancer: Diagnostic and therapeutic implications.
    Dasgupta A, Chen KH, Wu D, Hoskin V, Mewburn J, Lima PDA, Parlow LRG, Hindmarch CCT, Martin A, Sykes EA, Tayade C, Lightbody ED, Madarnas Y, SenGupta SK, Elliott BE, Nicol CJB, Archer SL.

    01/23/2021
    In health, MiD49 regulate Drp1-mediated fission, whereas in disease, epigenetic upregulation of MiD49 increases mitotic fission, which drives pathological proliferation and apoptosis resistance

    Epigenetic Dysregulation of the Dynamin-Related Protein 1 Binding Partners MiD49 and MiD51 Increases Mitotic Mitochondrial Fission and Promotes Pulmonary Arterial Hypertension: Mechanistic and Therapeutic Implications.
    Chen KH, Dasgupta A, Lin J, Potus F, Bonnet S, Iremonger J, Fu J, Mewburn J, Wu D, Dunham-Snary K, Theilmann AL, Jing ZC, Hindmarch C, Ormiston ML, Lawrie A, Archer SL., Free PMC Article

    10/5/2019
    cryo-electron microscopy structure of full-length human DRP1 co-assembled with MID49 and an analysis of structure- and disease-based mutations

    Structural basis of mitochondrial receptor binding and constriction by DRP1.
    Kalia R, Wang RY, Yusuf A, Thomas PV, Agard DA, Shaw JM, Frost A., Free PMC Article

    12/22/2018
    Knockdown of MIEF2 reduces DOX-induced mitochondrial fission and apoptosis in cardiomyocytes and in vivo. Also, knockdown of MIEF2 protects heart from DOX-induced cardiotoxicity. Our study identifies a novel pathway composed of Foxo3a and MIEF2 that mediates DOX cardiotoxicity.

    Foxo3a inhibits mitochondrial fission and protects against doxorubicin-induced cardiotoxicity by suppressing MIEF2.
    Zhou L, Li R, Liu C, Sun T, Htet Aung LH, Chen C, Gao J, Zhao Y, Wang K.

    12/16/2017
    MiD49 and MiD51 recruit inactive forms of Drp1 in mitochondrial fission. [review]

    The role of Drp1 adaptor proteins MiD49 and MiD51 in mitochondrial fission: implications for human disease.
    Atkins K, Dasgupta A, Chen KH, Mewburn J, Archer SL.

    07/8/2017
    These findings and data showing MARCH5-dependent degradation of MiD49 upon stress support the possibility that MARCH5 regulation of MiD49 is a novel mechanism controlling mitochondrial fission and, consequently, the cellular response to stress.

    Mitochondrial E3 ubiquitin ligase MARCH5 controls mitochondrial fission and cell sensitivity to stress-induced apoptosis through regulation of MiD49 protein.
    Xu S, Cherok E, Das S, Li S, Roelofs BA, Ge SX, Polster BM, Boyman L, Lederer WJ, Wang C, Karbowski M., Free PMC Article

    12/17/2016
    The results indicate that Drp1-dependent mitochondrial fission through MiD49/MiD51 regulates cristae remodeling during intrinsic apoptosis.

    Drp1-dependent mitochondrial fission via MiD49/51 is essential for apoptotic cristae remodeling.
    Otera H, Miyata N, Kuge O, Mihara K., Free PMC Article

    07/16/2016
    MIEF1 and MIEF2 are differentially expressed in human tissues during development

    The mitochondrial elongation factors MIEF1 and MIEF2 exert partially distinct functions in mitochondrial dynamics.
    Liu T, Yu R, Jin SB, Han L, Lendahl U, Zhao J, Nistér M.

    12/28/2013
    MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and suggest that they provide specificity to the division of mitochondria.

    Adaptor proteins MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission.
    Palmer CS, Elgass KD, Parton RG, Osellame LD, Stojanovski D, Ryan MT., Free PMC Article

    11/30/2013
    we find that either MiD49 or MiD51 can mediate Drp1 recruitment and mitochondrial fission in the absence of Fis1 and Mff.

    Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission.
    Losón OC, Song Z, Chen H, Chan DC., Free PMC Article

    09/14/2013
    MiD49/51 are new mediators of mitochondrial division affecting Drp1 action at mitochondria.

    MiD49 and MiD51, new components of the mitochondrial fission machinery.
    Palmer CS, Osellame LD, Laine D, Koutsopoulos OS, Frazier AE, Ryan MT, Palmer CS, Osellame LD, Laine D, Koutsopoulos OS, Frazier AE, Ryan MT., Free PMC Articles: PMC3128275, PMC3128275

    09/17/2011
    Mitochondrial outer membrane protein that recruits fission mediator Drp1 to the mitochondrial surface.

    MiD49 and MiD51, new components of the mitochondrial fission machinery.
    Palmer CS, Osellame LD, Laine D, Koutsopoulos OS, Frazier AE, Ryan MT, Palmer CS, Osellame LD, Laine D, Koutsopoulos OS, Frazier AE, Ryan MT., Free PMC Articles: PMC3128275, PMC3128275

    06/28/2011
    Smith-Magenis syndrome is caused by a de novo deletion on chromosome 17.

    Communicative competence and behavioural phenotype in children with Smith-Magenis syndrome.
    Sarimski K.

    01/21/2010
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