메뉴 건너뛰기




Volumn 100, Issue , 2014, Pages 115-124

Methylation of the DNA/RNA-binding protein Kin17 by METTL22 affects its association with chromatin

Author keywords

BUD13; Chromatin; Kin17; Lysine methylation; METTL22; Winged helix

Indexed keywords

BUD13 PROTEIN; DNA BINDING PROTEIN; KIN17 PROTEIN; LYSINE; METHYLTRANSFERASE; METTL22 PROTEIN; PROTEIN; RNA BINDING PROTEIN; SMALL NUCLEAR RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG; CHROMATIN; KIN PROTEIN, HUMAN; METTL22 PROTEIN, HUMAN;

EID: 84897050176     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.10.008     Document Type: Article
Times cited : (31)

References (43)
  • 1
    • 0024571620 scopus 로고
    • KIN, a mammalian nuclear protein immunologically related to E. coli RecA protein
    • Angulo J.F., Moreau P.L., Maunoury R., Laporte J., Hill A.M., Bertolotti R., et al. KIN, a mammalian nuclear protein immunologically related to E. coli RecA protein. Mutat Res 1989, 217:123-134.
    • (1989) Mutat Res , vol.217 , pp. 123-134
    • Angulo, J.F.1    Moreau, P.L.2    Maunoury, R.3    Laporte, J.4    Hill, A.M.5    Bertolotti, R.6
  • 3
    • 0033863436 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the human KIN17 cDNA encoding a component of the UVC response that is conserved among metazoans
    • Kannouche P., Mauffrey P., Pinon-Lataillade G., Mattei M.G., Sarasin A., Daya-Grosjean L., et al. Molecular cloning and characterization of the human KIN17 cDNA encoding a component of the UVC response that is conserved among metazoans. Carcinogenesis 2000, 21:1701-1710.
    • (2000) Carcinogenesis , vol.21 , pp. 1701-1710
    • Kannouche, P.1    Mauffrey, P.2    Pinon-Lataillade, G.3    Mattei, M.G.4    Sarasin, A.5    Daya-Grosjean, L.6
  • 4
    • 0031816433 scopus 로고    scopus 로고
    • The nuclear concentration of kin17, a mouse protein that binds to curved DNA, increases during cell proliferation and after UV irradiation
    • Kannouche P., Pinon-Lataillade G., Tissier A., Chevalier-Lagente O., Sarasin A., Mezzina M., et al. The nuclear concentration of kin17, a mouse protein that binds to curved DNA, increases during cell proliferation and after UV irradiation. Carcinogenesis 1998, 19:781-789.
    • (1998) Carcinogenesis , vol.19 , pp. 781-789
    • Kannouche, P.1    Pinon-Lataillade, G.2    Tissier, A.3    Chevalier-Lagente, O.4    Sarasin, A.5    Mezzina, M.6
  • 5
    • 0037166249 scopus 로고    scopus 로고
    • Ionizing radiation triggers chromatin-bound kin17 complex formation in human cells
    • Biard D.S., Miccoli L., Despras E., Frobert Y., Creminon C., Angulo J.F. Ionizing radiation triggers chromatin-bound kin17 complex formation in human cells. J Biol Chem 2002, 277:19156-19165.
    • (2002) J Biol Chem , vol.277 , pp. 19156-19165
    • Biard, D.S.1    Miccoli, L.2    Despras, E.3    Frobert, Y.4    Creminon, C.5    Angulo, J.F.6
  • 7
    • 0038386062 scopus 로고    scopus 로고
    • Depletion of KIN17, a human DNA replication protein, increases the radiosensitivity of RKO cells
    • Despras E., Miccoli L., Creminon C., Rouillard D., Angulo J.F., Biard D.S. Depletion of KIN17, a human DNA replication protein, increases the radiosensitivity of RKO cells. Radiat Res 2003, 159:748-758.
    • (2003) Radiat Res , vol.159 , pp. 748-758
    • Despras, E.1    Miccoli, L.2    Creminon, C.3    Rouillard, D.4    Angulo, J.F.5    Biard, D.S.6
  • 8
    • 0032730354 scopus 로고    scopus 로고
    • Overexpression of kin17 protein disrupts nuclear morphology and inhibits the growth of mammalian cells
    • Kannouche P., Angulo J.F. Overexpression of kin17 protein disrupts nuclear morphology and inhibits the growth of mammalian cells. J Cell Sci 1999, 112(Pt 19):3215-3224.
    • (1999) J Cell Sci , vol.112 , Issue.PART 19 , pp. 3215-3224
    • Kannouche, P.1    Angulo, J.F.2
  • 9
    • 0033179428 scopus 로고    scopus 로고
    • Ectopic expression of (Mm)Kin17 protein inhibits cell proliferation of human tumor-derived cells
    • Biard D.S., Kannouche P., Lannuzel-Drogou C., Mauffrey P., Apiou F., Angulo J.F. Ectopic expression of (Mm)Kin17 protein inhibits cell proliferation of human tumor-derived cells. Exp Cell Res 1999, 250:499-509.
    • (1999) Exp Cell Res , vol.250 , pp. 499-509
    • Biard, D.S.1    Kannouche, P.2    Lannuzel-Drogou, C.3    Mauffrey, P.4    Apiou, F.5    Angulo, J.F.6
  • 10
    • 17644425300 scopus 로고    scopus 로고
    • The human stress-activated protein kin17 belongs to the multiprotein DNA replication complex and associates in vivo with mammalian replication origins
    • Miccoli L., Frouin I., Novac O., Di Paola D., Harper F., Zannis-Hadjopoulos M., et al. The human stress-activated protein kin17 belongs to the multiprotein DNA replication complex and associates in vivo with mammalian replication origins. Mol Cell Biol 2005, 25:3814-3830.
    • (2005) Mol Cell Biol , vol.25 , pp. 3814-3830
    • Miccoli, L.1    Frouin, I.2    Novac, O.3    Di Paola, D.4    Harper, F.5    Zannis-Hadjopoulos, M.6
  • 11
    • 33750939601 scopus 로고    scopus 로고
    • A tandem of SH3-like domains participates in RNA binding in KIN17, a human protein activated in response to genotoxics
    • le Maire A., Schiltz M., Stura E.A., Pinon-Lataillade G., Couprie J., Moutiez M., et al. A tandem of SH3-like domains participates in RNA binding in KIN17, a human protein activated in response to genotoxics. J Mol Biol 2006, 364:764-776.
    • (2006) J Mol Biol , vol.364 , pp. 764-776
    • le Maire, A.1    Schiltz, M.2    Stura, E.A.3    Pinon-Lataillade, G.4    Couprie, J.5    Moutiez, M.6
  • 13
    • 0037073946 scopus 로고    scopus 로고
    • Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome
    • Makarov E.M., Makarova O.V., Urlaub H., Gentzel M., Will C.L., Wilm M., et al. Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome. Science 2002, 298:2205-2208.
    • (2002) Science , vol.298 , pp. 2205-2208
    • Makarov, E.M.1    Makarova, O.V.2    Urlaub, H.3    Gentzel, M.4    Will, C.L.5    Wilm, M.6
  • 14
    • 0036674269 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • Rappsilber J., Ryder U., Lamond A.I., Mann M. Large-scale proteomic analysis of the human spliceosome. Genome Res 2002, 12:1231-1245.
    • (2002) Genome Res , vol.12 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 16
    • 0025029381 scopus 로고
    • The fork head domain: a novel DNA binding motif of eukaryotic transcription factors?
    • Weigel D., Jackle H. The fork head domain: a novel DNA binding motif of eukaryotic transcription factors?. Cell 1990, 63:455-456.
    • (1990) Cell , vol.63 , pp. 455-456
    • Weigel, D.1    Jackle, H.2
  • 17
    • 36448970858 scopus 로고    scopus 로고
    • Solution structure of the region 51-160 of human KIN17 reveals an atypical winged helix domain
    • Carlier L., Couprie J., le Maire A., Guilhaudis L., Milazzo-Segalas I., Courcon M., et al. Solution structure of the region 51-160 of human KIN17 reveals an atypical winged helix domain. Protein Sci 2007, 16:2750-2755.
    • (2007) Protein Sci , vol.16 , pp. 2750-2755
    • Carlier, L.1    Couprie, J.2    le Maire, A.3    Guilhaudis, L.4    Milazzo-Segalas, I.5    Courcon, M.6
  • 18
    • 84873513121 scopus 로고    scopus 로고
    • A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity
    • Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B. A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet 2013, 9:e1003210.
    • (2013) PLoS Genet , vol.9
    • Cloutier, P.1    Lavallee-Adam, M.2    Faubert, D.3    Blanchette, M.4    Coulombe, B.5
  • 19
    • 34447321025 scopus 로고    scopus 로고
    • Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme
    • Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C., et al. Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme. Mol Cell 2007, 27:262-274.
    • (2007) Mol Cell , vol.27 , pp. 262-274
    • Jeronimo, C.1    Forget, D.2    Bouchard, A.3    Li, Q.4    Chua, G.5    Poitras, C.6
  • 20
    • 0037244282 scopus 로고    scopus 로고
    • Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1
    • Cote J., Boisvert F.M., Boulanger M.C., Bedford M.T., Richard S. Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1. Mol Biol Cell 2003, 14:274-287.
    • (2003) Mol Biol Cell , vol.14 , pp. 274-287
    • Cote, J.1    Boisvert, F.M.2    Boulanger, M.C.3    Bedford, M.T.4    Richard, S.5
  • 21
    • 19744379989 scopus 로고    scopus 로고
    • Multimerization of expressed protein-arginine methyltransferases during the growth and differentiation of rat liver
    • Lim Y., Kwon Y.H., Won N.H., Min B.H., Park I.S., Paik W.K., et al. Multimerization of expressed protein-arginine methyltransferases during the growth and differentiation of rat liver. Biochim Biophys Acta 2005, 1723:240-247.
    • (2005) Biochim Biophys Acta , vol.1723 , pp. 240-247
    • Lim, Y.1    Kwon, Y.H.2    Won, N.H.3    Min, B.H.4    Park, I.S.5    Paik, W.K.6
  • 22
    • 4444281106 scopus 로고    scopus 로고
    • Sequential Peptide Affinity (SPA) system for the identification of mammalian and bacterial protein complexes
    • Zeghouf M., Li J., Butland G., Borkowska A., Canadien V., Richards D., et al. Sequential Peptide Affinity (SPA) system for the identification of mammalian and bacterial protein complexes. Proteome Res 2004, 3:463-468.
    • (2004) Proteome Res , vol.3 , pp. 463-468
    • Zeghouf, M.1    Li, J.2    Butland, G.3    Borkowska, A.4    Canadien, V.5    Richards, D.6
  • 23
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: a general procedure of protein complex purification
    • Puig O., Caspary F., Rigaut G., Rutz B., Bouveret E., Bragado-Nilsson E., et al. The tandem affinity purification (TAP) method: a general procedure of protein complex purification. Methods 2001, 24:218-229.
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1    Caspary, F.2    Rigaut, G.3    Rutz, B.4    Bouveret, E.5    Bragado-Nilsson, E.6
  • 24
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G., Shevchenko A., Rutz B., Wilm M., Mann M., Seraphin B. A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol 1999, 17:1030-1032.
    • (1999) Nat Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 25
    • 67849097183 scopus 로고    scopus 로고
    • High-resolution mapping of the protein interaction network for the human transcription machinery and affinity purification of RNA polymerase II-associated complexes
    • Cloutier P., Al-Khoury R., Lavallee-Adam M., Faubert D., Jiang H., Poitras C., et al. High-resolution mapping of the protein interaction network for the human transcription machinery and affinity purification of RNA polymerase II-associated complexes. Methods 2009, 48:381-386.
    • (2009) Methods , vol.48 , pp. 381-386
    • Cloutier, P.1    Al-Khoury, R.2    Lavallee-Adam, M.3    Faubert, D.4    Jiang, H.5    Poitras, C.6
  • 26
    • 84874089670 scopus 로고    scopus 로고
    • Discovery of cell compartment specific protein-protein interactions using affinity purification combined with tandem mass spectrometry
    • Lavallee-Adam M., Rousseau J., Domecq C., Bouchard A., Forget D., Faubert D., et al. Discovery of cell compartment specific protein-protein interactions using affinity purification combined with tandem mass spectrometry. J Proteome Res 2013, 12:272-281.
    • (2013) J Proteome Res , vol.12 , pp. 272-281
    • Lavallee-Adam, M.1    Rousseau, J.2    Domecq, C.3    Bouchard, A.4    Forget, D.5    Faubert, D.6
  • 27
    • 84878500590 scopus 로고    scopus 로고
    • Immunomodulatory impact of leishmania-induced macrophage exosomes: a comparative proteomic and functional analysis
    • Hassani K., Olivier M. Immunomodulatory impact of leishmania-induced macrophage exosomes: a comparative proteomic and functional analysis. PLoS Negl Trop Dis 2013, 7:e2185.
    • (2013) PLoS Negl Trop Dis , vol.7
    • Hassani, K.1    Olivier, M.2
  • 29
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 30
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: tool for the unification of biology. The Gene Ontology Consortium
    • Ashburner M., Ball C.A., Blake J.A., Botstein D., Butler H., Cherry J.M., et al. Gene ontology: tool for the unification of biology. The Gene Ontology Consortium. Nat Genet 2000, 25:25-29.
    • (2000) Nat Genet , vol.25 , pp. 25-29
    • Ashburner, M.1    Ball, C.A.2    Blake, J.A.3    Botstein, D.4    Butler, H.5    Cherry, J.M.6
  • 31
    • 0142242155 scopus 로고    scopus 로고
    • Nuclear export of ERK3 by a CRM1-dependent mechanism regulates its inhibitory action on cell cycle progression
    • Julien C., Coulombe P., Meloche S. Nuclear export of ERK3 by a CRM1-dependent mechanism regulates its inhibitory action on cell cycle progression. J Biol Chem 2003, 278:42615-42624.
    • (2003) J Biol Chem , vol.278 , pp. 42615-42624
    • Julien, C.1    Coulombe, P.2    Meloche, S.3
  • 32
    • 84881540559 scopus 로고    scopus 로고
    • Nuclear import of RNA polymerase II is coupled with nucleocytoplasmic shuttling of the RNA polymerase II-associated protein
    • Forget D., Lacombe A.A., Cloutier P., Lavallee-Adam M., Blanchette M., Coulombe B. Nuclear import of RNA polymerase II is coupled with nucleocytoplasmic shuttling of the RNA polymerase II-associated protein. Nucleic Acids Res 2013, 2.
    • (2013) Nucleic Acids Res , vol.2
    • Forget, D.1    Lacombe, A.A.2    Cloutier, P.3    Lavallee-Adam, M.4    Blanchette, M.5    Coulombe, B.6
  • 33
    • 34547114282 scopus 로고    scopus 로고
    • Redundant role of DEAD box proteins p68 (Ddx5) and p72/p82 (Ddx17) in ribosome biogenesis and cell proliferation
    • Jalal C., Uhlmann-Schiffler H., Stahl H. Redundant role of DEAD box proteins p68 (Ddx5) and p72/p82 (Ddx17) in ribosome biogenesis and cell proliferation. Nucleic Acids Res 2007, 35:3590-3601.
    • (2007) Nucleic Acids Res , vol.35 , pp. 3590-3601
    • Jalal, C.1    Uhlmann-Schiffler, H.2    Stahl, H.3
  • 34
    • 0030296854 scopus 로고    scopus 로고
    • KOW: a novel motif linking a bacterial transcription factor with ribosomal proteins
    • Kyrpides N.C., Woese C.R., Ouzounis C.A. KOW: a novel motif linking a bacterial transcription factor with ribosomal proteins. Trends Biochem Sci 1996, 21:425-426.
    • (1996) Trends Biochem Sci , vol.21 , pp. 425-426
    • Kyrpides, N.C.1    Woese, C.R.2    Ouzounis, C.A.3
  • 35
    • 77951819088 scopus 로고    scopus 로고
    • Systematic analysis of human protein complexes identifies chromosome segregation proteins
    • Hutchins J.R., Toyoda Y., Hegemann B., Poser I., Heriche J.K., Sykora M.M., et al. Systematic analysis of human protein complexes identifies chromosome segregation proteins. Science 2010, 328:593-599.
    • (2010) Science , vol.328 , pp. 593-599
    • Hutchins, J.R.1    Toyoda, Y.2    Hegemann, B.3    Poser, I.4    Heriche, J.K.5    Sykora, M.M.6
  • 36
    • 0035162931 scopus 로고    scopus 로고
    • A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae
    • Ni L., Snyder M. A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae. Mol Biol Cell 2001, 12:2147-2170.
    • (2001) Mol Biol Cell , vol.12 , pp. 2147-2170
    • Ni, L.1    Snyder, M.2
  • 37
    • 11244276986 scopus 로고    scopus 로고
    • Proteomic analysis identifies a new complex required for nuclear pre-mRNA retention and splicing
    • Dziembowski A., Ventura A.P., Rutz B., Caspary F., Faux C., Halgand F., et al. Proteomic analysis identifies a new complex required for nuclear pre-mRNA retention and splicing. EMBO J 2004, 23:4847-4856.
    • (2004) EMBO J , vol.23 , pp. 4847-4856
    • Dziembowski, A.1    Ventura, A.P.2    Rutz, B.3    Caspary, F.4    Faux, C.5    Halgand, F.6
  • 39
    • 84875498382 scopus 로고
    • Regulation of molecular chaperones through post-translational modifications: decrypting the chaperone code
    • Cloutier P., Coulombe B. Regulation of molecular chaperones through post-translational modifications: decrypting the chaperone code. Biochim Biophys Acta 1829, 2013:443-454.
    • (1829) Biochim Biophys Acta , vol.2013 , pp. 443-454
    • Cloutier, P.1    Coulombe, B.2
  • 40
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Hornbeck P.V., Kornhauser J.M., Tkachev S., Zhang B., Skrzypek E., Murray B., et al. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res 2012, 40:D261-D270.
    • (2012) Nucleic Acids Res , vol.40
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6
  • 41
    • 84859223099 scopus 로고    scopus 로고
    • The role of protein arginine methylation in mRNP dynamics
    • Yu M.C. The role of protein arginine methylation in mRNP dynamics. Mol Biol Int 2011, 2011:163827.
    • (2011) Mol Biol Int , vol.2011 , pp. 163827
    • Yu, M.C.1
  • 42
    • 80053327867 scopus 로고    scopus 로고
    • Up-regulation of kin17 is essential for proliferation of breast cancer
    • Zeng T., Gao H., Yu P., He H., Ouyang X., Deng L., et al. Up-regulation of kin17 is essential for proliferation of breast cancer. PLoS One 2011, 6:e25343.
    • (2011) PLoS One , vol.6
    • Zeng, T.1    Gao, H.2    Yu, P.3    He, H.4    Ouyang, X.5    Deng, L.6
  • 43
    • 84867026199 scopus 로고    scopus 로고
    • Enhanced HSP70 lysine methylation promotes proliferation of cancer cells through activation of Aurora kinase B
    • Cho H.S., Shimazu T., Toyokawa G., Daigo Y., Maehara Y., Hayami S., et al. Enhanced HSP70 lysine methylation promotes proliferation of cancer cells through activation of Aurora kinase B. Nat Commun 2012, 3:1072.
    • (2012) Nat Commun , vol.3 , pp. 1072
    • Cho, H.S.1    Shimazu, T.2    Toyokawa, G.3    Daigo, Y.4    Maehara, Y.5    Hayami, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.