379
Views
21
CrossRef citations to date
0
Altmetric
Original Articles: Research

Low expression of ASH2L protein correlates with a favorable outcome in acute myeloid leukemia

, , , , , & show all
Pages 1207-1218 | Received 10 Apr 2016, Accepted 05 Sep 2016, Published online: 13 Oct 2016

References

  • Butler JS, Dent SY. The role of chromatin modifiers in normal and malignant hematopoiesis. Blood. 2013;121:3076–3084.
  • Milne TA, Briggs SD, Brock HW, et al. MLL targets SET domain methyltransferase activity to Hox gene promoters. Mol Cell. 2002;10:1107–1117.
  • Ziemin-van der Poel S, McCabe NR, Gill HJ, et al. Identification of a gene, MLL, that spans the breakpoint in 11q23 translocations associated with human leukemias. Proc Natl Acad Sci USA. 1991;88:10735–10739.
  • Tkachuk DC, Kohler S, Cleary ML. Involvement of a homolog of Drosophila Trithorax by 11q23 chromosomal translocations in acute leukemias. Cell. 1992;71:691–700.
  • Chen CS, Sorensen PH, Domer PH, et al. Molecular rearrangements on chromosome 11q23 predominate in infant acute lymphoblastic leukemia and are associated with specific biologic variables and poor outcome. Blood. 1993;81:2386–2393.
  • Dou Y, Milne TA, Ruthenburg AJ, et al. Regulation of MLL1 H3K4 methyltransferase activity by its core components. Nat Struct Mol Biol. 2006;13:713–719.
  • Steward MM, Lee JS, O'Donovan A, et al. Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes. Nat Struct Mol Biol. 2006;13:852–854.
  • Patel A, Dharmarajan V, Vought VE, et al. On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J Biol Chem. 2009;284:24242–24256.
  • Yang Z, Augustin J, Hu J, et al. Physical interactions and functional coordination between the core subunits of set1/Mll complexes and the reprogramming factors. PLoS One. 2015;10:e0145336. doi: 10.1371/journal.pone.0145336.
  • Tan CC, Sindhu KV, Li S, et al. Transcription factor Ap2delta associates with Ash2l and ALR, a trithorax family histone methyltransferase, to activate Hoxc8 transcription. Proc Natl Acad Sci USA. 2008;105:7472–7477.
  • Ikegawa S, Isomura M, Koshizuka Y, et al. Cloning and characterization of ASH2L and Ash2l, human and mouse homologs of the Drosophila ash2 gene. Cytogenet Cell Genet. 1999;84:167–172.
  • Stoller JZ, Huang L, Tan CC, et al. Ash2l interacts with Tbx1 and is required during early embryogenesis. Exp Biol Med (Maywood). 2010;235:569–576.
  • Wang J, Zhou Y, Yin B, et al. ASH2L: alternative splicing and downregulation during induced megakaryocytic differentiation of multipotential leukemia cell lines. J Mol Med (Berl). 2001;79:399–405.
  • Demers C, Chaturvedi CP, Ranish JA, et al. Activator-mediated recruitment of the MLL2 methyltransferase complex to the beta-globin locus. Mol Cell. 2007;27:573–584.
  • Zhang P, Chaturvedi CP, Tremblay V, et al. A phosphorylation switch on RbBP5 regulates histone H3 Lys4 methylation. Genes Dev. 2015;29:123–128.
  • Luscher-Firzlaff J, Gawlista I, Vervoorts J, et al. The human trithorax protein hASH2 functions as an oncoprotein. Cancer Res. 2008;68:749–758.
  • Ullius A, Luscher-Firzlaff J, Costa IG, et al. The interaction of MYC with the trithorax protein ASH2L promotes gene transcription by regulating H3K27 modification. Nucleic Acids Res. 2014;42:6901–6920.
  • Butler JS, Zurita-Lopez CI, Clarke SG, et al. Protein-arginine methyltransferase 1 (PRMT1) methylates ASH2L, a shared component of mammalian histone H3K4 methyltransferase complexes. J Biol Chem. 2011;286:12234–12244.
  • Chang YI, Hua WK, Yao CL, et al. Protein-arginine methyltransferase 1 suppresses megakaryocytic differentiation via modulation of the p38 MAPK pathway in K562 cells. J Biol Chem. 2010;285:20595–20606.
  • Cheung N, Chan LC, Thompson A, et al. Protein arginine-methyltransferase-dependent oncogenesis. Nat Cell Biol. 2007;9:1208–1215.
  • Wang L, Pal S, Sif S. Protein arginine methyltransferase 5 suppresses the transcription of the RB family of tumor suppressors in leukemia and lymphoma cells. Mol Cell Biol. 2008;28:6262–6277.
  • Kornblau SM, Singh N, Qiu Y, et al. Highly phosphorylated FOXO3A is an adverse prognostic factor in acute myeloid leukemia. Clin Cancer Res. 2010;16:1865–1874.
  • Kornblau SM, Qiu YH, Zhang N, et al. Abnormal expression of FLI1 protein is an adverse prognostic factor in acute myeloid leukemia. Blood. 2011;118:5604–5612.
  • Kornblau SM, Coombes KR. Use of reverse phase protein microarrays to study protein expression in leukemia: technical and methodological lessons learned. Methods Mol Biol. 2011;785:141–155.
  • Tibes R, Qiu Y, Lu Y, et al. Reverse phase protein array: validation of a novel proteomic technology and utility for analysis of primary leukemia specimens and hematopoietic stem cells. Mol Cancer Ther. 2006;5:2512–2521.
  • Ortega A, Niksic M, Bachi A, et al. Biochemical function of female-lethal (2)D/Wilms' tumor suppressor-1-associated proteins in alternative pre-mRNA splicing. J Biol Chem. 2003;278:3040–3047.
  • Venables JP, Koh CS, Froehlich U, et al. Multiple and specific mRNA processing targets for the major human hnRNP proteins. Mol Cell Biol. 2008;28:6033–6043.
  • Stirewalt DL, Radich JP. The role of FLT3 in haematopoietic malignancies. Nat Rev Cancer. 2003;3:650–665.
  • Smith CC, Wang Q, Chin CS, et al. Validation of ITD mutations in FLT3 as a therapeutic target in human acute myeloid leukaemia. Nature. 2012;485:260–263.
  • Lindstrom MS. NPM1/B23: a multifunctional chaperone in ribosome biogenesis and chromatin remodeling. Biochem Res Int. 2011;2011:195209. doi: 10.1155/2011/195209.
  • Okuwaki M, Matsumoto K, Tsujimoto M, et al. Function of nucleophosmin/B23, a nucleolar acidic protein, as a histone chaperone. FEBS Lett. 2001;506:272–276.
  • Murano K, Okuwaki M, Hisaoka M, et al. Transcription regulation of the rRNA gene by a multifunctional nucleolar protein, B23/nucleophosmin, through its histone chaperone activity. Mol Cell Biol. 2008;28:3114–3126.
  • Falini B, Gionfriddo I, Cecchetti F, et al. Acute myeloid leukemia with mutated nucleophosmin (NPM1): any hope for a targeted therapy?. Blood Rev. 2011;25:247–254.
  • Greer EL, Maures TJ, Hauswirth AG, et al. Members of the H3K4 trimethylation complex regulate lifespan in a germline-dependent manner in C. elegans. Nature. 2010;466:383–387.
  • Greer EL, Maures TJ, Ucar D, et al. Transgenerational epigenetic inheritance of longevity in Caenorhabditis elegans. Nature. 2011;479:365–371.
  • Ali A, Veeranki SN, Tyagi S. A SET-domain-independent role of WRAD complex in cell-cycle regulatory function of mixed lineage leukemia. Nucleic Acids Res. 2014;42:7611–7624.
  • Guertin DA, Guntur KV, Bell GW, et al. Functional genomics identifies TOR-regulated genes that control growth and division. Curr Biol. 2006;16:958–970.
  • Bomsztyk K, Denisenko O, Ostrowski J. hnRNP K: one protein multiple processes. Bioessays. 2004;26:629–638.
  • Bansal H, Yihua Q, Iyer SP, et al. WTAP is a novel oncogenic protein in acute myeloid leukemia. Leukemia. 2014;28:1171–1174.
  • Chen Y, Wan B, Wang KC, et al. Crystal structure of the N-terminal region of human ASH2L shows a winged-helix motif involved in DNA binding. EMBO Rep. 2011;12:797–803.
  • Sarvan S, Avdic V, Tremblay V, et al. Crystal structure of the trithorax group protein ASH2L reveals a forkhead-like DNA binding domain. Nat Struct Mol Biol. 2011;18:857–859.
  • Chang YI, Hsu SC, Chau GY, et al. Identification of the methylation preference region in heterogeneous nuclear ribonucleoprotein K by protein arginine methyltransferase 1 and its implication in regulating nuclear/cytoplasmic distribution. Biochem Biophys Res Commun. 2011;404:865–869.
  • Ostareck-Lederer A, Ostareck DH, Rucknagel KP, et al. Asymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src. J Biol Chem. 2006;281:11115–11125.
  • Briggs SD, Bryk M, Strahl BD, et al. Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae. Genes Dev. 2001;15:3286–3295.
  • Bryk M, Briggs SD, Strahl BD, et al. Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism. Curr Biol. 2002;12:165–170.
  • Fingerman IM, Wu CL, Wilson BD, et al. Global loss of Set1-mediated H3 Lys4 trimethylation is associated with silencing defects in Saccharomyces cerevisiae. J Biol Chem. 2005;280:28761–28765.
  • Falini B, Martelli MP, Bolli N, et al. Acute myeloid leukemia with mutated nucleophosmin (NPM1): is it a distinct entity?. Blood. 2011;117:1109–1120.
  • Falini B, Bolli N, Liso A, et al. Altered nucleophosmin transport in acute myeloid leukemia with mutated NPM1: molecular basis and clinical implications. Leukemia. 2009;23:1731–1743.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.