U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    MAF1 MAF1 homolog, negative regulator of RNA polymerase III [ Homo sapiens (human) ]

    Gene ID: 84232, updated on 17-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Maf1 suppression of ATF5-dependent mitochondrial unfolded protein response contributes to rapamycin-induced radio-sensitivity in lung cancer cell line A549.

    Maf1 suppression of ATF5-dependent mitochondrial unfolded protein response contributes to rapamycin-induced radio-sensitivity in lung cancer cell line A549.
    Lai C, Zhang J, Tan Z, Shen LF, Zhou RR, Zhang YY., Free PMC Article

    07/24/2021
    results identify the ubiquitin proteasome pathway and CUL2 as important regulators of MAF1 levels; they suggest that decreases in MAF1 protein underlie chemoresistance in HCC and perhaps other cancers and point to an important role for MAF1 and RNA pol III-mediated transcription in chemosensitivity and apoptosis

    The RNA polymerase III repressor MAF1 is regulated by ubiquitin-dependent proteasome degradation and modulates cancer drug resistance and apoptosis.
    Wang X, Rusin A, Walkey CJ, Lin JJ, Johnson DL., Free PMC Article

    07/18/2020
    Structural basis for RNA polymerase III transcription repression by Maf1 in humans and yeast has been uncovered.

    Structural basis for RNA polymerase III transcription repression by Maf1.
    Vorländer MK, Baudin F, Moir RD, Wetzel R, Hagen WJH, Willis IM, Müller CW., Free PMC Article

    04/18/2020
    High expression levels of MAF1 homolog, negative regulator of RNA Pol III (MAF1) is associated with advanced tumor depth, lymph node metastasis, distant metastasis and poor prognosis of colorectal cancer (CRC). MAF1 knockdown suppresses chemoresistance and migration of CRC cancer cells. High expression levels of MAF1 is an independent prognostic indicator in microsatellite instabilitypositive CRC.

    Involvement of MAF1 homolog, negative regulator of RNA polymerase III in colorectal cancer progression.
    Hokonohara K, Nishida N, Miyoshi N, Takahashi H, Haraguchi N, Hata T, Matsuda C, Mizushima T, Doki Y, Mori M., Free PMC Article

    05/25/2019
    can act as a transcriptional activator for PTEN, which is important for MAF1's tumor-suppressor function

    MAF1 suppresses AKT-mTOR signaling and liver cancer through activation of PTEN transcription.
    Li Y, Tsang CK, Wang S, Li XX, Yang Y, Fu L, Huang W, Li M, Wang HY, Zheng XF., Free PMC Article

    07/22/2017
    Repression of Pol III recruitment and transcription are tightly linked to MAF1, which selectively localizes at Pol III loci, even under serum-replete conditions, and increasingly targets transcribing Pol III in response to serum starvation

    Human MAF1 targets and represses active RNA polymerase III genes by preventing recruitment rather than inducing long-term transcriptional arrest.
    Orioli A, Praz V, Lhôte P, Hernandez N., Free PMC Article

    03/18/2017
    MAF1, RNF7 and SETD3 are identified as PCNA-associated proteins in human cells and given this interaction with PCNA, Maf1, RNF7, and SetD3 are potentially involved in DNA replication, DNA repair, or associated processes.

    A fluorescent bimolecular complementation screen reveals MAF1, RNF7 and SETD3 as PCNA-associated proteins in human cells.
    Cooper SE, Hodimont E, Green CM., Free PMC Article

    05/21/2016
    These results reveal a novel mechanism by which MAF1 and Pol III regulate the activity of the CDKN1A-encoding gene transcribed by Pol II.

    MAF1 represses CDKN1A through a Pol III-dependent mechanism.
    Lee YL, Li YC, Su CH, Chiao CH, Lin IH, Hsu MT., Free PMC Article

    03/12/2016
    novel role for Maf1 in suppressing both lipid biogenesis and tumor formation; Maf1 elicits these biological responses through its ability to repress genes that that synthesize lipids and regulate biosynthetic capacity.

    Maf1 is a novel target of PTEN and PI3K signaling that negatively regulates oncogenesis and lipid metabolism.
    Palian BM, Rohira AD, Johnson SA, He L, Zheng N, Dubeau L, Stiles BL, Johnson DL., Free PMC Article

    12/19/2015
    Studies on Maf1 regulation up until now have focused on posttranslational mechanisms, notably phosphorylation, which controls Maf1 localization (in yeast) and its interaction with the polymerase (in yeast and humans)

    Regulating maf1 expression and its expanding biological functions.
    Moir RD, Willis IM., Free PMC Article

    07/4/2015
    SUMOylation has a role in controlling Maf1 and RNA pol III-mediated transcription

    Covalent small ubiquitin-like modifier (SUMO) modification of Maf1 protein controls RNA polymerase III-dependent transcription repression.
    Rohira AD, Chen CY, Allen JR, Johnson DL., Free PMC Article

    09/14/2013
    Recovery of RNA polymerase III transcription from the glycerol-repressed state: revisiting the role of protein kinase CK2 in Maf1 phosphoregulation.

    Recovery of RNA polymerase III transcription from the glycerol-repressed state: revisiting the role of protein kinase CK2 in Maf1 phosphoregulation.
    Moir RD, Lee J, Willis IM., Free PMC Article

    11/24/2012
    The TOR pathway controls another aspect of Pol III transcription that is closely linked to MAF1, as it depends on the presence of MAF1.

    MAF1: a new target of mTORC1.
    Michels AA.

    07/2/2011
    an important role of CK2-mediated Maf1 phosphorylation in triggering Pol III activation.

    Casein kinase II-mediated phosphorylation of general repressor Maf1 triggers RNA polymerase III activation.
    Graczyk D, Debski J, Muszyńska G, Bretner M, Lefebvre O, Boguta M., Free PMC Article

    05/28/2011
    Data relate Pol III transcription inhibition to Maf1 structural changes.

    Full repression of RNA polymerase III transcription requires interaction between two domains of its negative regulator Maf1.
    Gajda A, Towpik J, Steuerwald U, Müller CW, Lefebvre O, Boguta M., Free PMC Article

    02/26/2011
    Maf1, a repressor that binds and inhibits pol III, is phosphorylated in a mTOR-dependent manner both in vitro and in vivo at serine 75, a site that contributes to its function as a transcriptional inhibitor.

    mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and targets their repressor Maf1.
    Kantidakis T, Ramsbottom BA, Birch JL, Dowding SN, White RJ., Free PMC Article

    08/16/2010
    mTOR inhibition led to an increase in the occupancy of Maf1 on a set of Pol III-dependent genes, with concomitant reduction in the binding of Pol III and Brf1

    Requirement of the mTOR kinase for the regulation of Maf1 phosphorylation and control of RNA polymerase III-dependent transcription in cancer cells.
    Shor B, Wu J, Shakey Q, Toral-Barza L, Shi C, Follettie M, Yu K., Free PMC Article

    06/28/2010
    Maf1 can be co-immunoprecipitated with pol III and associates in vitro with two pol III subunits, the largest subunit RPC1 and the alpha-like subunit RPAC2. Maf1 represses pol III transcription in vitro and in vivo.

    Maf1, a new player in the regulation of human RNA polymerase III transcription.
    Reina JH, Azzouz TN, Hernandez N., Free PMC Article

    03/22/2010
    The human Maf1 protein negatively regulates transcription by all three nuclear Pols. Changes in Maf1 expression affect Pol I- and Pol III-dependent transcription in human glioblastoma lines.

    Mammalian Maf1 is a negative regulator of transcription by all three nuclear RNA polymerases.
    Johnson SS, Zhang C, Fromm J, Willis IM, Johnson DL.

    01/21/2010
    represses RNA polymerase III transcription via TFIIIB, specifically through the TFIIB family members Brf1 and Brf2

    Human Maf1 negatively regulates RNA polymerase III transcription via the TFIIB family members Brf1 and Brf2.
    Rollins J, Veras I, Cabarcas S, Willis I, Schramm L., Free PMC Article

    01/21/2010
    Functional studies of the yeast counterpart.

    Maf1 is an essential mediator of diverse signals that repress RNA polymerase III transcription.
    Upadhya R, Lee J, Willis IM.

    08/6/2004
    Functional studies of the yeast counterpart.

    Maf1p, a negative effector of RNA polymerase III in Saccharomyces cerevisiae.
    Pluta K, Lefebvre O, Martin NC, Smagowicz WJ, Stanford DR, Ellis SR, Hopper AK, Sentenac A, Boguta M., Free PMC Article

    08/6/2004
    firstprevious page of 1 nextlast