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    RUVBL2 RuvB like AAA ATPase 2 [ Homo sapiens (human) ]

    Gene ID: 10856, updated on 5-May-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Adenovirus E1A binding to DCAF10 targets proteasomal degradation of RUVBL1/2 AAA+ ATPases required for quaternary assembly of multiprotein machines, innate immunity, and responses to metabolic stress.

    Adenovirus E1A binding to DCAF10 targets proteasomal degradation of RUVBL1/2 AAA+ ATPases required for quaternary assembly of multiprotein machines, innate immunity, and responses to metabolic stress.
    Zemke NR, Hsu E, Barshop WD, Sha J, Wohlschlegel JA, Berk AJ., Free PMC Article

    01/3/2024
    Assembly of the asymmetric human gamma-tubulin ring complex by RUVBL1-RUVBL2 AAA ATPase.

    Assembly of the asymmetric human γ-tubulin ring complex by RUVBL1-RUVBL2 AAA ATPase.
    Zimmermann F, Serna M, Ezquerra A, Fernandez-Leiro R, Llorca O, Luders J.

    04/30/2022
    RuvB-Like Protein 2 Interacts with the NS1 Protein of Influenza A Virus and Affects Apoptosis That Is Counterbalanced by Type I Interferons.

    RuvB-Like Protein 2 Interacts with the NS1 Protein of Influenza A Virus and Affects Apoptosis That Is Counterbalanced by Type I Interferons.
    Wang Y, Zhou J, Mackintosh SG, Du Y., Free PMC Article

    01/22/2022
    HEATR1, a novel interactor of Pontin/Reptin, stabilizes Pontin/Reptin and promotes cell proliferation of oral squamous cell carcinoma.

    HEATR1, a novel interactor of Pontin/Reptin, stabilizes Pontin/Reptin and promotes cell proliferation of oral squamous cell carcinoma.
    Nakamura A, Kakihara Y, Funayama A, Haga K, Mikami T, Kobayashi D, Yoshida Y, Izumi K, Kobayashi T, Saeki M.

    08/14/2021
    Novel HIF-2alpha interaction with Reptin52 impairs HIF-2 transcriptional activity and EPO secretion.

    Novel HIF-2α interaction with Reptin52 impairs HIF-2 transcriptional activity and EPO secretion.
    Gkotinakou IM, Befani C, Samiotaki M, Panayotou G, Liakos P.

    08/14/2021
    Regulation of RUVBL1-RUVBL2 AAA-ATPases by the nonsense-mediated mRNA decay factor DHX34, as evidenced by Cryo-EM.

    Regulation of RUVBL1-RUVBL2 AAA-ATPases by the nonsense-mediated mRNA decay factor DHX34, as evidenced by Cryo-EM.
    López-Perrote A, Hug N, González-Corpas A, Rodríguez CF, Serna M, García-Martín C, Boskovic J, Fernandez-Leiro R, Caceres JF, Llorca O., Free PMC Article

    03/20/2021
    NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2 during box C/D snoRNP biogenesis.

    NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2 during box C/D snoRNP biogenesis.
    Abel Y, Paiva ACF, Bizarro J, Chagot ME, Santo PE, Robert MC, Quinternet M, Vandermoere F, Sousa PMF, Fort P, Charpentier B, Manival X, Bandeiras TM, Bertrand E, Verheggen C., Free PMC Article

    02/6/2021
    These data demonstrate that RUVBL2 is essential for the oncogenic function of c-MYB in AML by governing inhibition of myeloid differentiation. They also indicate that targeting the control of c-MYB function by RUVBL2 is a promising approach to developing future anti-AML therapies.

    The AAA+ATPase RUVBL2 is essential for the oncogenic function of c-MYB in acute myeloid leukemia.
    Armenteros-Monterroso E, Zhao L, Gasparoli L, Brooks T, Pearce K, Mansour MR, Martens JHA, de Boer J, Williams O., Free PMC Article

    05/30/2020
    We identify RUVBL1 and RUVBL2 as novel interactors of Ebola virus NP and EBOV NP recruitment of the R2TP complex, which may provide novel targets for broad-acting anti-EBOV therapeutics.

    Identification of RUVBL1 and RUVBL2 as Novel Cellular Interactors of the Ebola Virus Nucleoprotein.
    Morwitzer MJ, Tritsch SR, Cazares LH, Ward MD, Nuss JE, Bavari S, Reid SP., Free PMC Article

    02/22/2020
    Analytical ultracentrifugation and cryo electron microscopy analyses performed on hsRuvBL2 highlight an oligomer plasticity that possibly reflects different physiological conformations of the protein in the cell, as well as that single-stranded DNA (ssDNA) can promote the oligomerization of monomeric hsRuvBL2.

    X-ray structure of full-length human RuvB-Like 2 - mechanistic insights into coupling between ATP binding and mechanical action.
    Silva STN, Brito JA, Arranz R, Sorzano CÓS, Ebel C, Doutch J, Tully MD, Carazo JM, Carrascosa JL, Matias PM, Bandeiras TM., Free PMC Article

    11/9/2019
    the INO80 complex, including Ino80 and actin-related proteins, is assembled around a single RUVBL1 (Tip49a) and RUVBL2 (Tip49b) AAA+ heterohexamer

    Cryo-EM structures of the human INO80 chromatin-remodeling complex.
    Aramayo RJ, Willhoft O, Ayala R, Bythell-Douglas R, Wigley DB, Zhang X., Free PMC Article

    07/27/2019
    Reptin directly interacted with histone deacetylase 1 (HDAC1) as the critical mechanism driving non-small cell lung cancer (NSCLC) tumour progression. Pharmacological disruption of the Reptin/HDAC1 complex resulted in a substantial decrease in NSCLC cell proliferation and induced significant sensitisation to cisplatin.

    Reptin drives tumour progression and resistance to chemotherapy in nonsmall cell lung cancer.
    Mikesch JH, Schwammbach D, Hartmann W, Schmidt LH, Schliemann C, Angenendt L, Wiewrodt R, Marra A, Thoennissen NH, Wardelmann E, Köhler G, Lenz G, Müller-Tidow C, Berdel WE, Arteaga MF.

    06/15/2019
    These results suggest a role of Reptin and Pontin in Salivary gland cancer tumor progression and/or patient survival.

    AAA+ ATPases Reptin and Pontin as potential diagnostic and prognostic biomarkers in salivary gland cancer - a short report.
    Mikesch JH, Hartmann W, Angenendt L, Huber O, Schliemann C, Arteaga MF, Wardelmann E, Rudack C, Berdel WE, Stenner M, Grünewald I.

    05/18/2019
    The interaction between RUVBL1/RUVBL2 and the U5 small nuclear ribonucleoprotein is mostly mediated by the previously uncharacterized factor ZNHIT2.

    R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 to regulate assembly of U5 small nuclear ribonucleoprotein.
    Cloutier P, Poitras C, Durand M, Hekmat O, Fiola-Masson É, Bouchard A, Faubert D, Chabot B, Coulombe B., Free PMC Article

    11/24/2018
    Mep1A is overexpressed in most hepatocellular carcinomas and induces tumor cell migration and invasion. Mep1A expression is regulated by Reptin, and Mep1A mediates Reptin-induced migration.

    Metalloproteinase meprin α regulates migration and invasion of human hepatocarcinoma cells and is a mediator of the oncoprotein Reptin.
    Breig O, Yates M, Neaud V, Couchy G, Grigoletto A, Lucchesi C, Prox J, Zucman-Rossi J, Becker-Pauly C, Rosenbaum J., Free PMC Article

    03/3/2018
    Reptin silencing did not affect the tyrosine phosphorylation of the insulin receptor nor of IRS1, but it enhanced the tyrosine phosphorylation of the p85 subunit of PI3K.

    Reptin regulates insulin-stimulated Akt phosphorylation in hepatocellular carcinoma via the regulation of SHP-1/PTPN6.
    Raymond AA, Javary J, Breig O, Neaud V, Rosenbaum J.

    09/30/2017
    Overall, POLG interactome mapping identifies novel proteins which support mitochondrial biogenesis and a potential novel mitochondrial isoform of Ruvbl2.

    Characterizing the mitochondrial DNA polymerase gamma interactome by BioID identifies Ruvbl2 localizes to the mitochondria.
    Liyanage SU, Coyaud E, Laurent EM, Hurren R, Maclean N, Wood SR, Kazak L, Shamas-Din A, Holt I, Raught B, Schimmer A.

    05/13/2017
    The authors report that HIV-1 exploits the host factor RuvB-like 2 (RVB2) to balance relative expression of Gag and Env for efficient production of infectious virions.

    HIV-1 Exploits the Host Factor RuvB-like 2 to Balance Viral Protein Expression.
    Mu X, Fu Y, Zhu Y, Wang X, Xuan Y, Shang H, Goff SP, Gao G.

    05/7/2016
    by means of molecular docking approaches we first modeled the structures of hetero-hexameric TIP49 ( TIP49a and TIP49b )complexes with short ds-DNA fragments (20 base pairs with different GC content) within the central channel of hexameric ring

    [DYNAMICS AND MECHANISMS OF INTERACTION OF HETERO-HEXAMERIC TIP49a/b COMPLEXES WITH DS-DNA].
    Afanasyeva AS, Yakimov AP, Grigoriev MY, Petukhov MG.

    03/26/2016
    Data suggest that overexpression of Reptin in hepatocellular carcinoma (HCC) could be a factor of resistance to treatment.

    Reptin regulates DNA double strand breaks repair in human hepatocellular carcinoma.
    Raymond AA, Benhamouche S, Neaud V, Di Martino J, Javary J, Rosenbaum J., Free PMC Article

    01/16/2016
    RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils.

    RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils.
    Zaarur N, Xu X, Lestienne P, Meriin AB, McComb M, Costello CE, Newnam GP, Ganti R, Romanova NV, Shanmugasundaram M, Silva ST, Bandeiras TM, Matias PM, Lobachev KS, Lednev IK, Chernoff YO, Sherman MY., Free PMC Article

    12/5/2015
    results reveal a novel mechanism for the control of NF-kappaB pathway by cytoplasmic Reptin

    Reptin physically interacts with p65 and represses NF-κB activation.
    Qiu H, Gao Y, Mao D.

    10/3/2015
    The results suggests that a potential mechanism for the role of RuvBL1-RuvBL2 in maintaining genome integrity is through controlling the cellular abundance of Fanconi anaemia core complex.

    Abundance of the Fanconi anaemia core complex is regulated by the RuvBL1 and RuvBL2 AAA+ ATPases.
    Rajendra E, Garaycoechea JI, Patel KJ, Passmore LA., Free PMC Article

    05/16/2015
    Reptin and Pontin oligomerization and activity are modulated through histone H3 N-terminal tail interaction.

    Reptin and Pontin oligomerization and activity are modulated through histone H3 N-terminal tail interaction.
    Queval R, Papin C, Dalvai M, Bystricky K, Humbert O., Free PMC Article

    03/7/2015
    these findings suggest that YY1-RuvBL1-RuvBL2 complexes could contribute to functions beyond transcription, and we show that YY1 and the ATPase activity of RuvBL2 are required for RAD51 foci formation during homologous recombination.

    Structure of Yin Yang 1 oligomers that cooperate with RuvBL1-RuvBL2 ATPases.
    López-Perrote A, Alatwi HE, Torreira E, Ismail A, Ayora S, Downs JA, Llorca O., Free PMC Article

    12/20/2014
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