메뉴 건너뛰기




Volumn 44, Issue 6, 2016, Pages 435-441

Arginine methyltransferases in normal and malignant hematopoiesis

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASM PROTEIN; DNA; HISTONE DEACETYLASE 1; MIXED LINEAGE LEUKEMIA PROTEIN; N(G) METHYLARGININE; PRMT4 PROTEIN; PRMT5 PROTEIN; PRMT6 PROTEIN; PRMT7 PROTEIN; PROTEIN; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN P53; PROTEIN SM; PROTEIN SWI; RNA; SMALL INTERFERING RNA; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR E2F; TRANSCRIPTION FACTOR NANOG; TRANSCRIPTION FACTOR RUNX1; TRANSCRIPTION FACTOR SIN3A; TRANSCRIPTION FACTOR SNF; TRANSCRIPTION FACTOR SOX2; UNCLASSIFIED DRUG; ISOPROTEIN; PRMT2 PROTEIN, HUMAN; SIGNAL PEPTIDE;

EID: 84964957431     PISSN: 0301472X     EISSN: 18732399     Source Type: Journal    
DOI: 10.1016/j.exphem.2016.03.009     Document Type: Review
Times cited : (49)

References (72)
  • 1
    • 84926609739 scopus 로고    scopus 로고
    • Comprehensive identification of arginine methylation in primary T cells reveals regulatory roles in cell signalling
    • Geoghegan V., Guo A., Trudgian D., Thomas B., Acuto O. Comprehensive identification of arginine methylation in primary T cells reveals regulatory roles in cell signalling. Nature Commun 2015, 6:6758.
    • (2015) Nature Commun , vol.6 , pp. 6758
    • Geoghegan, V.1    Guo, A.2    Trudgian, D.3    Thomas, B.4    Acuto, O.5
  • 2
    • 84861494738 scopus 로고    scopus 로고
    • PRMT1 interacts with AML1-ETO to promote its transcriptional activation and progenitor cell proliferative potential
    • Shia W.J., Okumura A.J., Yan M., et al. PRMT1 interacts with AML1-ETO to promote its transcriptional activation and progenitor cell proliferative potential. Blood 2012, 119:4953-4962.
    • (2012) Blood , vol.119 , pp. 4953-4962
    • Shia, W.J.1    Okumura, A.J.2    Yan, M.3
  • 3
    • 84864235609 scopus 로고    scopus 로고
    • Correlation of SRSF1 and PRMT1 expression with clinical status of pediatric acute lymphoblastic leukemia
    • Zou L., Zhang H., Du C., et al. Correlation of SRSF1 and PRMT1 expression with clinical status of pediatric acute lymphoblastic leukemia. J Hematol Oncol 2012, 5:42.
    • (2012) J Hematol Oncol , vol.5 , pp. 42
    • Zou, L.1    Zhang, H.2    Du, C.3
  • 4
    • 84995512373 scopus 로고    scopus 로고
    • Arginine methyltransferases are regulated by Epstein-Barr virus in B cells and are differentially expressed in Hodgkin's lymphoma
    • Leonard S., Gordon N., Smith N., Rowe M., Murray P.G., Woodman C.B. Arginine methyltransferases are regulated by Epstein-Barr virus in B cells and are differentially expressed in Hodgkin's lymphoma. Pathogens 2012, 1:52-64.
    • (2012) Pathogens , vol.1 , pp. 52-64
    • Leonard, S.1    Gordon, N.2    Smith, N.3    Rowe, M.4    Murray, P.G.5    Woodman, C.B.6
  • 5
    • 78649638594 scopus 로고    scopus 로고
    • Dysregulation of PRMT1 and PRMT6, type I arginine methyltransferases, is involved in various types of human cancers
    • Yoshimatsu M., Toyokawa G., Hayami S., et al. Dysregulation of PRMT1 and PRMT6, type I arginine methyltransferases, is involved in various types of human cancers. Int J Cancer 2011, 128:562-573.
    • (2011) Int J Cancer , vol.128 , pp. 562-573
    • Yoshimatsu, M.1    Toyokawa, G.2    Hayami, S.3
  • 6
    • 84891008290 scopus 로고    scopus 로고
    • PRMT4 blocks myeloid differentiation by assembling a methyl-RUNX1-dependent repressor complex
    • Vu L.P., Perna F., Wang L., et al. PRMT4 blocks myeloid differentiation by assembling a methyl-RUNX1-dependent repressor complex. Cell Rep 2013, 5:1625-1638.
    • (2013) Cell Rep , vol.5 , pp. 1625-1638
    • Vu, L.P.1    Perna, F.2    Wang, L.3
  • 8
    • 53549103598 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 5 suppresses the transcription of the RB family of tumor suppressors in leukemia and lymphoma cells
    • 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.
    • (2008) Mol Cell Biol , vol.28 , pp. 6262-6277
    • Wang, L.1    Pal, S.2    Sif, S.3
  • 9
    • 34547741040 scopus 로고    scopus 로고
    • Low levels of miR-92b/96 induce PRMT5 translation and H3R8/H4R3 methylation in mantle cell lymphoma
    • Pal S., Baiocchi R.A., Byrd J.C., Grever M.R., Jacob S.T., Sif S. Low levels of miR-92b/96 induce PRMT5 translation and H3R8/H4R3 methylation in mantle cell lymphoma. EMBO J 2007, 26:3558-3569.
    • (2007) EMBO J , vol.26 , pp. 3558-3569
    • Pal, S.1    Baiocchi, R.A.2    Byrd, J.C.3    Grever, M.R.4    Jacob, S.T.5    Sif, S.6
  • 10
    • 0034045559 scopus 로고    scopus 로고
    • Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable
    • Pawlak M.R., Scherer C.A., Chen J., Roshon M.J., Ruley H.E. Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable. Mol Cell Biol 2000, 20:4859-4869.
    • (2000) Mol Cell Biol , vol.20 , pp. 4859-4869
    • Pawlak, M.R.1    Scherer, C.A.2    Chen, J.3    Roshon, M.J.4    Ruley, H.E.5
  • 11
    • 0034677814 scopus 로고    scopus 로고
    • PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells
    • Tang J., Frankel A., Cook R.J., et al. PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells. J Biol Chem 2000, 275:7723-7730.
    • (2000) J Biol Chem , vol.275 , pp. 7723-7730
    • Tang, J.1    Frankel, A.2    Cook, R.J.3
  • 12
    • 23944435995 scopus 로고    scopus 로고
    • Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications
    • Huang S., Litt M., Felsenfeld G. Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications. Genes Dev 2005, 19:1885-1893.
    • (2005) Genes Dev , vol.19 , pp. 1885-1893
    • Huang, S.1    Litt, M.2    Felsenfeld, G.3
  • 13
    • 2942612843 scopus 로고    scopus 로고
    • Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53
    • An W., Kim J., Roeder R.G. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell 2004, 117:735-748.
    • (2004) Cell , vol.117 , pp. 735-748
    • An, W.1    Kim, J.2    Roeder, R.G.3
  • 14
    • 40349113414 scopus 로고    scopus 로고
    • Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity
    • Zhao X., Jankovic V., Gural A., et al. Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity. Genes Dev 2008, 22:640-653.
    • (2008) Genes Dev , vol.22 , pp. 640-653
    • Zhao, X.1    Jankovic, V.2    Gural, A.3
  • 15
    • 84940601871 scopus 로고    scopus 로고
    • Loss of RUNX1/AML1 arginine-methylation impairs peripheral T cell homeostasis
    • Mizutani S., Yoshida T., Zhao X., Nimer S.D., Taniwaki M., Okuda T. Loss of RUNX1/AML1 arginine-methylation impairs peripheral T cell homeostasis. Br J Haematol 2015, 170:859-873.
    • (2015) Br J Haematol , vol.170 , pp. 859-873
    • Mizutani, S.1    Yoshida, T.2    Zhao, X.3    Nimer, S.D.4    Taniwaki, M.5    Okuda, T.6
  • 17
    • 84958817283 scopus 로고    scopus 로고
    • Targeting aberrant epigenetic networks mediated by PRMT1 and KDM4C in acute myeloid leukemia
    • Cheung N., Fung T.K., Zeisig B.B., et al. Targeting aberrant epigenetic networks mediated by PRMT1 and KDM4C in acute myeloid leukemia. Cancer Ccell 2016, 29:32-48.
    • (2016) Cancer Ccell , vol.29 , pp. 32-48
    • Cheung, N.1    Fung, T.K.2    Zeisig, B.B.3
  • 18
    • 80053900941 scopus 로고    scopus 로고
    • Frequent pathway mutations of splicing machinery in myelodysplasia
    • Yoshida K., Sanada M., Shiraishi Y., et al. Frequent pathway mutations of splicing machinery in myelodysplasia. Nature 2011, 478:64-69.
    • (2011) Nature , vol.478 , pp. 64-69
    • Yoshida, K.1    Sanada, M.2    Shiraishi, Y.3
  • 19
    • 84958212707 scopus 로고    scopus 로고
    • Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing
    • Zhang L., Tran N.T., Su H., et al. Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing. eLife 2015, 4.
    • (2015) eLife , pp. 4
    • Zhang, L.1    Tran, N.T.2    Su, H.3
  • 20
    • 77953318366 scopus 로고    scopus 로고
    • CARM1 is required for proper control of proliferation and differentiation of pulmonary epithelial cells
    • O'Brien K.B., Alberich-Jorda M., Yadav N., et al. CARM1 is required for proper control of proliferation and differentiation of pulmonary epithelial cells. Development 2010, 137:2147-2156.
    • (2010) Development , vol.137 , pp. 2147-2156
    • O'Brien, K.B.1    Alberich-Jorda, M.2    Yadav, N.3
  • 21
    • 2942537778 scopus 로고    scopus 로고
    • Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-regulated phosphoprotein and deregulated early T cell development
    • Kim J., Lee J., Yadav N., et al. Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-regulated phosphoprotein and deregulated early T cell development. J Biol Chem 2004, 279:25339-25344.
    • (2004) J Biol Chem , vol.279 , pp. 25339-25344
    • Kim, J.1    Lee, J.2    Yadav, N.3
  • 22
    • 33846226977 scopus 로고    scopus 로고
    • Histone arginine methylation regulates pluripotency in the early mouse embryo
    • Torres-Padilla M.E., Parfitt D.E., Kouzarides T., Zernicka-Goetz M. Histone arginine methylation regulates pluripotency in the early mouse embryo. Nature 2007, 445:214-218.
    • (2007) Nature , vol.445 , pp. 214-218
    • Torres-Padilla, M.E.1    Parfitt, D.E.2    Kouzarides, T.3    Zernicka-Goetz, M.4
  • 23
    • 72849152508 scopus 로고    scopus 로고
    • CARM1 is required in embryonic stem cells to maintain pluripotency and resist differentiation
    • Wu Q., Bruce A.W., Jedrusik A., et al. CARM1 is required in embryonic stem cells to maintain pluripotency and resist differentiation. Stem Cells 2009, 27:2637-2645.
    • (2009) Stem Cells , vol.27 , pp. 2637-2645
    • Wu, Q.1    Bruce, A.W.2    Jedrusik, A.3
  • 24
    • 84866091538 scopus 로고    scopus 로고
    • Carm1 regulates Pax7 transcriptional activity through MLL1/2 recruitment during asymmetric satellite stem cell divisions
    • Kawabe Y., Wang Y.X., McKinnell I.W., Bedford M.T., Rudnicki M.A. Carm1 regulates Pax7 transcriptional activity through MLL1/2 recruitment during asymmetric satellite stem cell divisions. Cell Stem Cell 2012, 11:333-345.
    • (2012) Cell Stem Cell , vol.11 , pp. 333-345
    • Kawabe, Y.1    Wang, Y.X.2    McKinnell, I.W.3    Bedford, M.T.4    Rudnicki, M.A.5
  • 25
    • 33750342491 scopus 로고    scopus 로고
    • Signaling within a coactivator complex: Methylation of SRC-3/AIB1 is a molecular switch for complex disassembly
    • Feng Q., Yi P., Wong J., O'Malley B.W. Signaling within a coactivator complex: Methylation of SRC-3/AIB1 is a molecular switch for complex disassembly. Mol Cell Biol 2006, 26:7846-7857.
    • (2006) Mol Cell Biol , vol.26 , pp. 7846-7857
    • Feng, Q.1    Yi, P.2    Wong, J.3    O'Malley, B.W.4
  • 26
    • 33846001366 scopus 로고    scopus 로고
    • The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing
    • Cheng D., Cote J., Shaaban S., Bedford M.T. The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing. Mol Cell 2007, 25:71-83.
    • (2007) Mol Cell , vol.25 , pp. 71-83
    • Cheng, D.1    Cote, J.2    Shaaban, S.3    Bedford, M.T.4
  • 27
    • 84892427869 scopus 로고    scopus 로고
    • CARM1 methylates chromatin remodeling factor BAF155 to enhance tumor progression and metastasis
    • Wang L., Zhao Z., Meyer M.B., et al. CARM1 methylates chromatin remodeling factor BAF155 to enhance tumor progression and metastasis. Cancer Cell 2014, 25:21-36.
    • (2014) Cancer Cell , vol.25 , pp. 21-36
    • Wang, L.1    Zhao, Z.2    Meyer, M.B.3
  • 28
    • 77949568399 scopus 로고    scopus 로고
    • Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and SWI/SNF/Mediator implies an indexing transcription factor code
    • Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A. Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and SWI/SNF/Mediator implies an indexing transcription factor code. EMBO J 2010, 29:1105-1115.
    • (2010) EMBO J , vol.29 , pp. 1105-1115
    • Kowenz-Leutz, E.1    Pless, O.2    Dittmar, G.3    Knoblich, M.4    Leutz, A.5
  • 29
    • 0035980018 scopus 로고    scopus 로고
    • PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins
    • Branscombe T.L., Frankel A., Lee J.H., et al. PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. J Biol Chem 2001, 276:32971-32976.
    • (2001) J Biol Chem , vol.276 , pp. 32971-32976
    • Branscombe, T.L.1    Frankel, A.2    Lee, J.H.3
  • 30
    • 0033615656 scopus 로고    scopus 로고
    • The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity
    • Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., Pestka S. The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. J Biol Chem 1999, 274:31531-31542.
    • (1999) J Biol Chem , vol.274 , pp. 31531-31542
    • Pollack, B.P.1    Kotenko, S.V.2    He, W.3    Izotova, L.S.4    Barnoski, B.L.5    Pestka, S.6
  • 31
    • 84859977491 scopus 로고    scopus 로고
    • HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules
    • Bandyopadhyay S., Harris D.P., Adams G.N., et al. HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules. Mol Cell Biol 2012, 32:1202-1213.
    • (2012) Mol Cell Biol , vol.32 , pp. 1202-1213
    • Bandyopadhyay, S.1    Harris, D.P.2    Adams, G.N.3
  • 32
    • 57049087451 scopus 로고    scopus 로고
    • Arginine methylation regulates the p53 response
    • Jansson M., Durant S.T., Cho E.C., et al. Arginine methylation regulates the p53 response. Nat Cell Biol 2008, 10:1431-1439.
    • (2008) Nat Cell Biol , vol.10 , pp. 1431-1439
    • Jansson, M.1    Durant, S.T.2    Cho, E.C.3
  • 33
    • 31344465966 scopus 로고    scopus 로고
    • MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical and functional properties
    • Le Guezennec X., Vermeulen M., Brinkman A.B., et al. MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical and functional properties. Mol Cell Biol 2006, 26:843-851.
    • (2006) Mol Cell Biol , vol.26 , pp. 843-851
    • Le Guezennec, X.1    Vermeulen, M.2    Brinkman, A.B.3
  • 34
    • 0035846546 scopus 로고    scopus 로고
    • Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln
    • Meister G., Eggert C., Buhler D., Brahms H., Kambach C., Fischer U. Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Curr Biol 2001, 11:1990-1994.
    • (2001) Curr Biol , vol.11 , pp. 1990-1994
    • Meister, G.1    Eggert, C.2    Buhler, D.3    Brahms, H.4    Kambach, C.5    Fischer, U.6
  • 36
    • 0036845335 scopus 로고    scopus 로고
    • Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs
    • Meister G., Fischer U. Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs. EMBO J 2002, 21:5853-5863.
    • (2002) EMBO J , vol.21 , pp. 5853-5863
    • Meister, G.1    Fischer, U.2
  • 37
    • 44449137369 scopus 로고    scopus 로고
    • Deciphering the assembly pathway of Sm-class U snRNPs
    • Neuenkirchen N., Chari A., Fischer U. Deciphering the assembly pathway of Sm-class U snRNPs. FEBS Lett 2008, 582:1997-2003.
    • (2008) FEBS Lett , vol.582 , pp. 1997-2003
    • Neuenkirchen, N.1    Chari, A.2    Fischer, U.3
  • 38
    • 84883607837 scopus 로고    scopus 로고
    • Regulation of constitutive and alternative splicing by PRMT5 reveals a role for Mdm4 pre-mRNA in sensing defects in the spliceosomal machinery
    • Bezzi M., Teo S.X., Muller J., et al. Regulation of constitutive and alternative splicing by PRMT5 reveals a role for Mdm4 pre-mRNA in sensing defects in the spliceosomal machinery. Genes Dev 2013, 27:1903-1916.
    • (2013) Genes Dev , vol.27 , pp. 1903-1916
    • Bezzi, M.1    Teo, S.X.2    Muller, J.3
  • 39
    • 84933282444 scopus 로고    scopus 로고
    • MYC regulates the core pre-mRNA splicing machinery as an essential step in lymphomagenesis
    • Koh C.M., Bezzi M., Low D.H., et al. MYC regulates the core pre-mRNA splicing machinery as an essential step in lymphomagenesis. Nature 2015, 523:96-100.
    • (2015) Nature , vol.523 , pp. 96-100
    • Koh, C.M.1    Bezzi, M.2    Low, D.H.3
  • 40
    • 84865729111 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 5 is a potential oncoprotein that upregulates G1 cyclins/cyclin-dependent kinases and the phosphoinositide 3-kinase/AKT signaling cascade
    • Wei T.Y., Juan C.C., Hisa J.Y., et al. Protein arginine methyltransferase 5 is a potential oncoprotein that upregulates G1 cyclins/cyclin-dependent kinases and the phosphoinositide 3-kinase/AKT signaling cascade. Cancer Sci 2012, 103:1640-1650.
    • (2012) Cancer Sci , vol.103 , pp. 1640-1650
    • Wei, T.Y.1    Juan, C.C.2    Hisa, J.Y.3
  • 41
    • 84868159296 scopus 로고    scopus 로고
    • Crystal structure of the human PRMT5:MEP50 complex
    • Antonysamy S., Bonday Z., Campbell R.M., et al. Crystal structure of the human PRMT5:MEP50 complex. Proc Natl Acad Sci USA 2012, 109:17960-17965.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 17960-17965
    • Antonysamy, S.1    Bonday, Z.2    Campbell, R.M.3
  • 42
    • 78751526816 scopus 로고    scopus 로고
    • RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity
    • Guderian G., Peter C., Wiesner J., et al. RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity. J Biol Chem 2011, 286:1976-1986.
    • (2011) J Biol Chem , vol.286 , pp. 1976-1986
    • Guderian, G.1    Peter, C.2    Wiesner, J.3
  • 43
    • 43049084803 scopus 로고    scopus 로고
    • The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5
    • Lacroix M., El Messaoudi S., Rodier G., Le Cam A., Sardet C., Fabbrizio E. The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5. EMBO Rep 2008, 9:452-458.
    • (2008) EMBO Rep , vol.9 , pp. 452-458
    • Lacroix, M.1    El Messaoudi, S.2    Rodier, G.3    Le Cam, A.4    Sardet, C.5    Fabbrizio, E.6
  • 44
    • 79751486147 scopus 로고    scopus 로고
    • JAK2V617F-mediated phosphorylation of PRMT5 downregulates its methyltransferase activity and promotes myeloproliferation
    • Liu F., Zhao X., Perna F., et al. JAK2V617F-mediated phosphorylation of PRMT5 downregulates its methyltransferase activity and promotes myeloproliferation. Cancer Cell 2011, 19:283-294.
    • (2011) Cancer Cell , vol.19 , pp. 283-294
    • Liu, F.1    Zhao, X.2    Perna, F.3
  • 45
    • 84865429451 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 5 functions in opposite ways in the cytoplasm and nucleus of prostate cancer cells
    • Gu Z., Li Y., Lee P., Liu T., Wan C., Wang Z. Protein arginine methyltransferase 5 functions in opposite ways in the cytoplasm and nucleus of prostate cancer cells. PloS One 2012, 7(8):e44033.
    • (2012) PloS One , vol.7 , Issue.8 , pp. e44033
    • Gu, Z.1    Li, Y.2    Lee, P.3    Liu, T.4    Wan, C.5    Wang, Z.6
  • 46
    • 84871133298 scopus 로고    scopus 로고
    • Transcription factor positive regulatory domain 4 (PRDM4) recruits protein arginine methyltransferase 5 (PRMT5) to mediate histone arginine methylation and control neural stem cell proliferation and differentiation
    • Chittka A., Nitarska J., Grazini U., Richardson W.D. Transcription factor positive regulatory domain 4 (PRDM4) recruits protein arginine methyltransferase 5 (PRMT5) to mediate histone arginine methylation and control neural stem cell proliferation and differentiation. J Biol Chem 2012, 287:42995-43006.
    • (2012) J Biol Chem , vol.287 , pp. 42995-43006
    • Chittka, A.1    Nitarska, J.2    Grazini, U.3    Richardson, W.D.4
  • 47
    • 78650212707 scopus 로고    scopus 로고
    • Prmt5 is essential for early mouse development and acts in the cytoplasm to maintain ES cell pluripotency
    • Tee W.W., Pardo M., Theunissen T.W., et al. Prmt5 is essential for early mouse development and acts in the cytoplasm to maintain ES cell pluripotency. Genes Dev 2010, 24:2772-2777.
    • (2010) Genes Dev , vol.24 , pp. 2772-2777
    • Tee, W.W.1    Pardo, M.2    Theunissen, T.W.3
  • 48
    • 84941657778 scopus 로고    scopus 로고
    • Arginine methyltransferase PRMT5 is essential for sustaining normal adult hematopoiesis
    • Liu F., Cheng G., Hamard P.J., et al. Arginine methyltransferase PRMT5 is essential for sustaining normal adult hematopoiesis. J Clin Invest 2015, 125:3532-3544.
    • (2015) J Clin Invest , vol.125 , pp. 3532-3544
    • Liu, F.1    Cheng, G.2    Hamard, P.J.3
  • 49
    • 84939937365 scopus 로고    scopus 로고
    • The PRMT5 arginine methyltransferase: Many roles in development, cancer and beyond
    • Stopa N., Krebs J.E., Shechter D. The PRMT5 arginine methyltransferase: Many roles in development, cancer and beyond. Cell Mol Life Sci 2015, 72:2041-2059.
    • (2015) Cell Mol Life Sci , vol.72 , pp. 2041-2059
    • Stopa, N.1    Krebs, J.E.2    Shechter, D.3
  • 50
    • 84875499792 scopus 로고    scopus 로고
    • Overexpression of PRMT5 promotes tumor cell growth and is associated with poor disease prognosis in epithelial ovarian cancer
    • Bao X., Zhao S., Liu T., Liu Y., Liu Y., Yang X. Overexpression of PRMT5 promotes tumor cell growth and is associated with poor disease prognosis in epithelial ovarian cancer. J Histochem Cytochem 2013, 61:206-217.
    • (2013) J Histochem Cytochem , vol.61 , pp. 206-217
    • Bao, X.1    Zhao, S.2    Liu, T.3    Liu, Y.4    Liu, Y.5    Yang, X.6
  • 51
    • 84925302177 scopus 로고    scopus 로고
    • PRMT5 is required for lymphomagenesis triggered by multiple oncogenic drivers
    • Li Y., Chitnis N., Nakagawa H., et al. PRMT5 is required for lymphomagenesis triggered by multiple oncogenic drivers. Cancer Discovery 2015, 5:288-303.
    • (2015) Cancer Discovery , vol.5 , pp. 288-303
    • Li, Y.1    Chitnis, N.2    Nakagawa, H.3
  • 52
    • 84937397052 scopus 로고    scopus 로고
    • A selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL models
    • Chan-Penebre E., Kuplast K.G., Majer C.R., et al. A selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL models. Nat Chem Biol 2015, 11:432-437.
    • (2015) Nat Chem Biol , vol.11 , pp. 432-437
    • Chan-Penebre, E.1    Kuplast, K.G.2    Majer, C.R.3
  • 53
    • 84948410742 scopus 로고    scopus 로고
    • The dual epigenetic role of PRMT5 in acute myeloid leukemia: Gene activation and repression via histone arginine methylation
    • Tarighat S.S., Santhanam R., Frankhouser D., et al. The dual epigenetic role of PRMT5 in acute myeloid leukemia: Gene activation and repression via histone arginine methylation. Leukemia 2016, 30:789-799.
    • (2016) Leukemia , vol.30 , pp. 789-799
    • Tarighat, S.S.1    Santhanam, R.2    Frankhouser, D.3
  • 54
    • 84960916279 scopus 로고    scopus 로고
    • MTAP deletion confers enhanced dependency on the PRMT5 arginine methyltransferase in cancer cells
    • Kryukov G.V., Wilson F.H., Ruth J.R., et al. MTAP deletion confers enhanced dependency on the PRMT5 arginine methyltransferase in cancer cells. Science 2016, 351:1214-1218.
    • (2016) Science , vol.351 , pp. 1214-1218
    • Kryukov, G.V.1    Wilson, F.H.2    Ruth, J.R.3
  • 55
    • 84960885579 scopus 로고    scopus 로고
    • Disordered methionine metabolism in MTAP/CDKN2A deleted cancers leads to dependence on PRMT5
    • Mavrakis K.J., McDonald E.R., Schlabach M.R., et al. Disordered methionine metabolism in MTAP/CDKN2A deleted cancers leads to dependence on PRMT5. Science 2016, 351:1208-1213.
    • (2016) Science , vol.351 , pp. 1208-1213
    • Mavrakis, K.J.1    McDonald, E.R.2    Schlabach, M.R.3
  • 56
    • 35349030188 scopus 로고    scopus 로고
    • Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive
    • Guccione E., Bassi C., Casadio F., et al. Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive. Nature 2007, 449:933-937.
    • (2007) Nature , vol.449 , pp. 933-937
    • Guccione, E.1    Bassi, C.2    Casadio, F.3
  • 57
    • 37249026306 scopus 로고    scopus 로고
    • PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation
    • Hyllus D., Stein C., Schnabel K., et al. PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation. Genes Dev 2007, 21:3369-3380.
    • (2007) Genes Dev , vol.21 , pp. 3369-3380
    • Hyllus, D.1    Stein, C.2    Schnabel, K.3
  • 58
    • 41249088464 scopus 로고    scopus 로고
    • Arginine methylation of the histone H3 tail impedes effector binding
    • Iberg A.N., Espejo A., Cheng D., et al. Arginine methylation of the histone H3 tail impedes effector binding. J Biol Chem 2008, 283:3006-3010.
    • (2008) J Biol Chem , vol.283 , pp. 3006-3010
    • Iberg, A.N.1    Espejo, A.2    Cheng, D.3
  • 59
    • 84866246480 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 6 regulates embryonic stem cell identity
    • Lee Y.H., Ma H., Tan T.Z., et al. Protein arginine methyltransferase 6 regulates embryonic stem cell identity. Stem Cells Dev 2012, 21:2613-2622.
    • (2012) Stem Cells Dev , vol.21 , pp. 2613-2622
    • Lee, Y.H.1    Ma, H.2    Tan, T.Z.3
  • 60
    • 84878017819 scopus 로고    scopus 로고
    • Histone arginine methylation keeps RUNX1 target genes in an intermediate state
    • Herglotz J., Kuvardina O.N., Kolodziej S., et al. Histone arginine methylation keeps RUNX1 target genes in an intermediate state. Oncogene 2013, 32:2565-2575.
    • (2013) Oncogene , vol.32 , pp. 2565-2575
    • Herglotz, J.1    Kuvardina, O.N.2    Kolodziej, S.3
  • 61
    • 84930965759 scopus 로고    scopus 로고
    • RUNX1 represses the erythroid gene expression program during megakaryocytic differentiation
    • Kuvardina O.N., Herglotz J., Kolodziej S., et al. RUNX1 represses the erythroid gene expression program during megakaryocytic differentiation. Blood 2015, 125:3570-3579.
    • (2015) Blood , vol.125 , pp. 3570-3579
    • Kuvardina, O.N.1    Herglotz, J.2    Kolodziej, S.3
  • 62
    • 84868110617 scopus 로고    scopus 로고
    • Ablation of PRMT6 reveals a role as a negative transcriptional regulator of the p53 tumor suppressor
    • Neault M., Mallette F.A., Vogel G., Michaud-Levesque J., Richard S. Ablation of PRMT6 reveals a role as a negative transcriptional regulator of the p53 tumor suppressor. Nucleic Acids Res 2012, 40:9513-9521.
    • (2012) Nucleic Acids Res , vol.40 , pp. 9513-9521
    • Neault, M.1    Mallette, F.A.2    Vogel, G.3    Michaud-Levesque, J.4    Richard, S.5
  • 63
    • 84868148269 scopus 로고    scopus 로고
    • P53-Independent regulation of p21Waf1/Cip1 expression and senescence by PRMT6
    • Phalke S., Mzoughi S., Bezzi M., et al. p53-Independent regulation of p21Waf1/Cip1 expression and senescence by PRMT6. Nucleic Acids Res 2012, 40:9534-9542.
    • (2012) Nucleic Acids Res , vol.40 , pp. 9534-9542
    • Phalke, S.1    Mzoughi, S.2    Bezzi, M.3
  • 64
    • 84858040000 scopus 로고    scopus 로고
    • Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming omega-NG-monomethylated arginine residues
    • Zurita-Lopez C.I., Sandberg T., Kelly R., Clarke S.G. Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming omega-NG-monomethylated arginine residues. J Biol Chem 2012, 287:7859-7870.
    • (2012) J Biol Chem , vol.287 , pp. 7859-7870
    • Zurita-Lopez, C.I.1    Sandberg, T.2    Kelly, R.3    Clarke, S.G.4
  • 65
    • 84891757565 scopus 로고    scopus 로고
    • The International Mouse Phenotyping Consortium Web Portal, a unified point of access for knockout mice and related phenotyping data
    • Koscielny G., Yaikhom G., Iyer V., et al. The International Mouse Phenotyping Consortium Web Portal, a unified point of access for knockout mice and related phenotyping data. Nucleic Acids Res 2014, 42(Database issue):D802-D809.
    • (2014) Nucleic Acids Res , vol.42 , Issue.DATABASE ISSUE , pp. D802-D809
    • Koscielny, G.1    Yaikhom, G.2    Iyer, V.3
  • 66
    • 60549102666 scopus 로고    scopus 로고
    • Identification of genomic regions contributing to etoposide-induced cytotoxicity
    • Bleibel W.K., Duan S., Huang R.S., et al. Identification of genomic regions contributing to etoposide-induced cytotoxicity. Hum Genet 2009, 125:173-180.
    • (2009) Hum Genet , vol.125 , pp. 173-180
    • Bleibel, W.K.1    Duan, S.2    Huang, R.S.3
  • 67
    • 33750526034 scopus 로고    scopus 로고
    • Characterization of prmt7alpha and beta isozymes from Chinese hamster cells sensitive and resistant to topoisomerase II inhibitors
    • Gros L., Renodon-Corniere A., de Saint Vincent B.R., Feder M., Bujnicki J.M., Jacquemin-Sablon A. Characterization of prmt7alpha and beta isozymes from Chinese hamster cells sensitive and resistant to topoisomerase II inhibitors. Biochim Biophys Acta 2006, 1760:1646-1656.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 1646-1656
    • Gros, L.1    Renodon-Corniere, A.2    de Saint Vincent, B.R.3    Feder, M.4    Bujnicki, J.M.5    Jacquemin-Sablon, A.6
  • 68
    • 42049099046 scopus 로고    scopus 로고
    • Protein arginine (N)-methyl transferase 7 (PRMT7) as a potential target for the sensitization of tumor cells to camptothecins
    • Verbiest V., Montaudon D., Tautu M.T., et al. Protein arginine (N)-methyl transferase 7 (PRMT7) as a potential target for the sensitization of tumor cells to camptothecins. FEBS Lett 2008, 582:1483-1489.
    • (2008) FEBS Lett , vol.582 , pp. 1483-1489
    • Verbiest, V.1    Montaudon, D.2    Tautu, M.T.3
  • 69
    • 84865526587 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase delta catalytic subunit gene, POLD1
    • Karkhanis V., Wang L., Tae S., Hu Y.J., Imbalzano A.N., Sif S. Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase delta catalytic subunit gene, POLD1. J Biol Chem 2012, 287:29801-29814.
    • (2012) J Biol Chem , vol.287 , pp. 29801-29814
    • Karkhanis, V.1    Wang, L.2    Tae, S.3    Hu, Y.J.4    Imbalzano, A.N.5    Sif, S.6
  • 70
    • 34548356376 scopus 로고    scopus 로고
    • Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins
    • Gonsalvez G.B., Tian L., Ospina J.K., Boisvert F.M., Lamond A.I., Matera A.G. Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. J Cell Biol 2007, 178:733-740.
    • (2007) J Cell Biol , vol.178 , pp. 733-740
    • Gonsalvez, G.B.1    Tian, L.2    Ospina, J.K.3    Boisvert, F.M.4    Lamond, A.I.5    Matera, A.G.6
  • 71
    • 84871568905 scopus 로고    scopus 로고
    • Trans-tail regulation of MLL4-catalyzed H3K4 methylation by H4R3 symmetric dimethylation is mediated by a tandem PHD of MLL4
    • Dhar S.S., Lee S.H., Kan P.Y., et al. Trans-tail regulation of MLL4-catalyzed H3K4 methylation by H4R3 symmetric dimethylation is mediated by a tandem PHD of MLL4. Genes Dev 2012, 26:2749-2762.
    • (2012) Genes Dev , vol.26 , pp. 2749-2762
    • Dhar, S.S.1    Lee, S.H.2    Kan, P.Y.3
  • 72
    • 84938923517 scopus 로고    scopus 로고
    • Histone arginine methylation by PRMT7 controls germinal center formation via regulating Bcl6 transcription
    • Ying Z., Mei M., Zhang P., et al. Histone arginine methylation by PRMT7 controls germinal center formation via regulating Bcl6 transcription. J Immunol 2015, 195:1538-1547.
    • (2015) J Immunol , vol.195 , pp. 1538-1547
    • Ying, Z.1    Mei, M.2    Zhang, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.