메뉴 건너뛰기




Volumn 1754, Issue 1-2, 2005, Pages 14-24

The RIO kinases: An atypical protein kinase family required for ribosome biogenesis and cell cycle progression

Author keywords

ATP binding; Atypical protein kinase; Enzymatic activity; Ribosome biogenesis; Rio1; Rio2; Structure

Indexed keywords

ABC TRANSPORTER A1; BCR ABL PROTEIN; BROMODOMAIN KINASE; FAS ACTIVATED S T KINASE; HEAT SHOCK PROTEIN 22; PHOSPHOINOSITIDE 3 KINASE RELATED KINASE; PROTEIN KINASE; PYRUVATE DEHYDROGENASE; RIGHT OPEN READING FRAME 1 KINASE; STEROID RECEPTOR COACTIVATOR 1; TATA BINDING FACTOR ASSOCIATED FACTOR 1; TRANSCRIPTION INTERMEDIARY FACTOR I; UNCLASSIFIED DRUG;

EID: 29144535787     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.07.037     Document Type: Conference Paper
Times cited : (92)

References (50)
  • 3
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • D.R. Knighton, J.H. Zheng, L.F. Ten Eyck, N.H. Xuong, S.S. Taylor, and J.M. Sowadski Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase Science 253 1991 414 420
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Xuong, N.H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 4
    • 0029020282 scopus 로고
    • Protein kinases 6. the eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • S.K. Hanks, and T. Hunter Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification FASEB J. 9 1995 576 596
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 5
    • 0032560489 scopus 로고    scopus 로고
    • The structural basis for substrate recognition and control by protein kinases
    • L.N. Johnson, E.D. Lowe, M.E.M. Noble, and D.J. Owen The structural basis for substrate recognition and control by protein kinases FEBS Lett. 430 1998 1 11
    • (1998) FEBS Lett. , vol.430 , pp. 1-11
    • Johnson, L.N.1    Lowe, E.D.2    Noble, M.E.M.3    Owen, D.J.4
  • 6
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • L.N. Johnson, M.E. Noble, and D.J. Owen Active and inactive protein kinases: structural basis for regulation Cell 85 1996 149 158
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 7
    • 1842536165 scopus 로고    scopus 로고
    • Alpha-kinases: Analysis of the family and comparison with conventional protein kinases
    • D. Drennan, and A.G. Ryazanov Alpha-kinases: analysis of the family and comparison with conventional protein kinases Prog. Biophys. Mol. Biol. 85 2004 1 32
    • (2004) Prog. Biophys. Mol. Biol. , vol.85 , pp. 1-32
    • Drennan, D.1    Ryazanov, A.G.2
  • 9
    • 0030941654 scopus 로고    scopus 로고
    • Mapping of the novel protein kinase catalytic domain of Dictyostelium myosin II heavy chain kinase a
    • G.P. Cote, X. Luo, M.B. Murphy, and T.T. Egelhoff Mapping of the novel protein kinase catalytic domain of Dictyostelium myosin II heavy chain kinase A J. Biol. Chem. 272 1997 6846 6849
    • (1997) J. Biol. Chem. , vol.272 , pp. 6846-6849
    • Cote, G.P.1    Luo, X.2    Murphy, M.B.3    Egelhoff, T.T.4
  • 10
    • 0035131504 scopus 로고    scopus 로고
    • TRP-PLIK, a bifunctional protein with kinase and ion channel activities
    • L.W. Runnels, L. Yue, and D.E. Clapham TRP-PLIK, a bifunctional protein with kinase and ion channel activities Science 291 2001 1043 1047
    • (2001) Science , vol.291 , pp. 1043-1047
    • Runnels, L.W.1    Yue, L.2    Clapham, D.E.3
  • 11
    • 0035947077 scopus 로고    scopus 로고
    • Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity
    • H. Yamaguchi, M. Matsushita, A.C. Nairn, and J. Kuriyan Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity Mol. Cell 7 2001 1047 1057
    • (2001) Mol. Cell , vol.7 , pp. 1047-1057
    • Yamaguchi, H.1    Matsushita, M.2    Nairn, A.C.3    Kuriyan, J.4
  • 13
    • 0033565569 scopus 로고    scopus 로고
    • Cloning, expression and characterization of an A6-related protein
    • A. Rohwer, W. Kittstein, F. Marks, and M. Gschwendt Cloning, expression and characterization of an A6-related protein Eur. J. Biochem. 263 1999 518 525
    • (1999) Eur. J. Biochem. , vol.263 , pp. 518-525
    • Rohwer, A.1    Kittstein, W.2    Marks, F.3    Gschwendt, M.4
  • 14
    • 3242882820 scopus 로고    scopus 로고
    • PI 3-kinase related kinases: 'Big' players in stress-induced signaling pathways
    • R.T. Abraham PI 3-kinase related kinases: 'big' players in stress-induced signaling pathways DNA Repair 3 2004 883 887
    • (2004) DNA Repair , vol.3 , pp. 883-887
    • Abraham, R.T.1
  • 15
    • 0033581886 scopus 로고    scopus 로고
    • Structural insights into phosphoinositide 3-kinase catalysis and signalling
    • E.H. Walker, O. Perisic, C. Ried, L. Stephens, and R.L. Williams Structural insights into phosphoinositide 3-kinase catalysis and signalling Nature 402 1999 313 320
    • (1999) Nature , vol.402 , pp. 313-320
    • Walker, E.H.1    Perisic, O.2    Ried, C.3    Stephens, L.4    Williams, R.L.5
  • 16
    • 0031722706 scopus 로고    scopus 로고
    • Novel families of putative protein kinases in bacteria and archaea: Evolution of the "eukaryotic" protein kinase superfamily
    • C.J. Leonard, L. Aravind, and E.V. Koonin Novel families of putative protein kinases in bacteria and archaea: evolution of the "eukaryotic" protein kinase superfamily Genome Res. 8 1998 1038 1047
    • (1998) Genome Res. , vol.8 , pp. 1038-1047
    • Leonard, C.J.1    Aravind, L.2    Koonin, E.V.3
  • 17
    • 0030027058 scopus 로고    scopus 로고
    • A novel, mitogen-activated nuclear kinase is related to a Drosophila developmental regulator
    • G.V. Denis, and M.R. Green A novel, mitogen-activated nuclear kinase is related to a Drosophila developmental regulator Genes Dev. 10 1996 261 271
    • (1996) Genes Dev. , vol.10 , pp. 261-271
    • Denis, G.V.1    Green, M.R.2
  • 18
    • 0035434378 scopus 로고    scopus 로고
    • You bet-cha: A novel family of transcriptional regulators
    • B. Florence, and D.V. Faller You bet-cha: a novel family of transcriptional regulators Front Biosci. 6 2001 D1008 D1018
    • (2001) Front Biosci. , vol.6
    • Florence, B.1    Faller, D.V.2
  • 20
    • 0033876160 scopus 로고    scopus 로고
    • RING3 kinase transactivates promoters of cell cycle regulatory genes through E2F
    • G.V. Denis, C. Vaziri, N. Guo, and D.V. Faller RING3 kinase transactivates promoters of cell cycle regulatory genes through E2F Cell Growth Differ. 11 2000 417 424
    • (2000) Cell Growth Differ. , vol.11 , pp. 417-424
    • Denis, G.V.1    Vaziri, C.2    Guo, N.3    Faller, D.V.4
  • 22
    • 0023076865 scopus 로고
    • CDNA sequence for human bcr, the gene that translocates to the abl oncogene in chronic myeloid leukaemia
    • I.K. Hariharan, and J.M. Adams cDNA sequence for human bcr, the gene that translocates to the abl oncogene in chronic myeloid leukaemia EMBO J. 6 1987 115 119
    • (1987) EMBO J. , vol.6 , pp. 115-119
    • Hariharan, I.K.1    Adams, J.M.2
  • 23
    • 0025942490 scopus 로고
    • The BCR gene encodes a novel serine/threonine kinase activity within a single exon
    • Y. Maru, and O.N. Witte The BCR gene encodes a novel serine/threonine kinase activity within a single exon Cell 67 1991 459 468
    • (1991) Cell , vol.67 , pp. 459-468
    • Maru, Y.1    Witte, O.N.2
  • 24
    • 0037706860 scopus 로고    scopus 로고
    • The Bcr kinase downregulates Ras signaling by phosphorylating AF-6 and binding to its PDZ domain
    • G. Radziwill, R.A. Erdmann, U. Margelisch, and K. Moelling The Bcr kinase downregulates Ras signaling by phosphorylating AF-6 and binding to its PDZ domain Mol. Cell. Biol. 23 2003 4663 4672
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4663-4672
    • Radziwill, G.1    Erdmann, R.A.2    Margelisch, U.3    Moelling, K.4
  • 25
    • 0034682806 scopus 로고    scopus 로고
    • A novel human gene similar to the protein kinase (PK) coding domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) codes for a serine-threonine PK and is expressed in melanoma cells
    • C.C. Smith, Y.X. Yu, M. Kulka, and L. Aurelian A novel human gene similar to the protein kinase (PK) coding domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) codes for a serine-threonine PK and is expressed in melanoma cells J. Biol. Chem. 275 2000 25690 25699
    • (2000) J. Biol. Chem. , vol.275 , pp. 25690-25699
    • Smith, C.C.1    Yu, Y.X.2    Kulka, M.3    Aurelian, L.4
  • 26
    • 0030035137 scopus 로고    scopus 로고
    • ATP and SH3 binding sites in the protein kinase of the large subunit of herpes simplex virus type 2 of ribonucleotide reductase (ICP10)
    • J.W. Nelson, J. Zhu, C.C. Smith, M. Kulka, and L. Aurelian ATP and SH3 binding sites in the protein kinase of the large subunit of herpes simplex virus type 2 of ribonucleotide reductase (ICP10) J. Biol. Chem. 271 1996 17021 17027
    • (1996) J. Biol. Chem. , vol.271 , pp. 17021-17027
    • Nelson, J.W.1    Zhu, J.2    Smith, C.C.3    Kulka, M.4    Aurelian, L.5
  • 28
    • 0029126581 scopus 로고
    • Fas-activated serine/threonine kinase (FAST) phosphorylates TIA-1 during Fas-mediated apoptosis
    • Q. Tian, J. Taupin, S. Elledge, M. Robertson, and P. Anderson Fas-activated serine/threonine kinase (FAST) phosphorylates TIA-1 during Fas-mediated apoptosis J. Exp. Med. 182 1995 865 874
    • (1995) J. Exp. Med. , vol.182 , pp. 865-874
    • Tian, Q.1    Taupin, J.2    Elledge, S.3    Robertson, M.4    Anderson, P.5
  • 29
    • 0021099811 scopus 로고
    • Purification and properties of pyruvate dehydrogenase kinase from bovine kidney
    • L.R. Stepp, F.H. Pettit, S.J. Yeaman, and L.J. Reed Purification and properties of pyruvate dehydrogenase kinase from bovine kidney J. Biol. Chem. 258 1983 9454 9458
    • (1983) J. Biol. Chem. , vol.258 , pp. 9454-9458
    • Stepp, L.R.1    Pettit, F.H.2    Yeaman, S.J.3    Reed, L.J.4
  • 30
    • 0035980919 scopus 로고    scopus 로고
    • Regulation of mammalian pyruvate dehydrogenase complex by phosphorylation: Complexity of multiple phosphorylation sites and kinases
    • M.S. Patel, and L.G. Korotchkina Regulation of mammalian pyruvate dehydrogenase complex by phosphorylation: complexity of multiple phosphorylation sites and kinases Exp. Mol. Med. 33 2001 191 197
    • (2001) Exp. Mol. Med. , vol.33 , pp. 191-197
    • Patel, M.S.1    Korotchkina, L.G.2
  • 32
    • 0035949483 scopus 로고    scopus 로고
    • Structure of rat BCKD kinase: Nucleotide-induced domain communication in a mitochondrial protein kinase
    • M. Machius, J.L. Chuang, R.M. Wynn, D.R. Tomchick, and D.T. Chuang Structure of rat BCKD kinase: nucleotide-induced domain communication in a mitochondrial protein kinase Proc. Natl. Acad. Sci. 98 2001 11218 11223
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 11218-11223
    • MacHius, M.1    Chuang, J.L.2    Wynn, R.M.3    Tomchick, D.R.4    Chuang, D.T.5
  • 33
    • 0029669982 scopus 로고    scopus 로고
    • TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74
    • R. Dikstein, S. Ruppert, and R. Tjian TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74 Cell 84 1996 781 790
    • (1996) Cell , vol.84 , pp. 781-790
    • Dikstein, R.1    Ruppert, S.2    Tjian, R.3
  • 34
    • 0032059786 scopus 로고    scopus 로고
    • Functional analysis of the human TAFII250 N-terminal kinase domain
    • T. O'Brien, and R. Tjian Functional analysis of the human TAFII250 N-terminal kinase domain Mol. Cell 1 1998 905 911
    • (1998) Mol. Cell , vol.1 , pp. 905-911
    • O'Brien, T.1    Tjian, R.2
  • 36
    • 0036231380 scopus 로고    scopus 로고
    • Yeast Rio1p is the founding member of a novel subfamily of protein serine kinases involved in the control of cell cycle progression
    • M. Angermayr, A. Roidl, and W. Bandlow Yeast Rio1p is the founding member of a novel subfamily of protein serine kinases involved in the control of cell cycle progression Mol. Microbiol. 44 2002 309 324
    • (2002) Mol. Microbiol. , vol.44 , pp. 309-324
    • Angermayr, M.1    Roidl, A.2    Bandlow, W.3
  • 37
    • 0036100787 scopus 로고    scopus 로고
    • Lipopolysaccharide phosphorylating enzymes encoded in the genomes of Gram-negative bacteria are related to the eukaryotic protein kinases
    • A. Krupa, and N. Srinivasan Lipopolysaccharide phosphorylating enzymes encoded in the genomes of Gram-negative bacteria are related to the eukaryotic protein kinases Protein Sci. 11 2002 1580 1584
    • (2002) Protein Sci. , vol.11 , pp. 1580-1584
    • Krupa, A.1    Srinivasan, N.2
  • 38
    • 0037928101 scopus 로고    scopus 로고
    • Rio2p, an evolutionarily conserved, low abundant protein kinase essential for processing of 20 S Pre-rRNA in Saccharomyces cerevisiae
    • T.H. Geerlings, A.W. Faber, M.D. Bister, J.C. Vos, and H.A. Raue Rio2p, an evolutionarily conserved, low abundant protein kinase essential for processing of 20 S Pre-rRNA in Saccharomyces cerevisiae J. Biol. Chem. 278 2003 22537 22545
    • (2003) J. Biol. Chem. , vol.278 , pp. 22537-22545
    • Geerlings, T.H.1    Faber, A.W.2    Bister, M.D.3    Vos, J.C.4    Raue, H.A.5
  • 40
    • 0037373221 scopus 로고    scopus 로고
    • Late cytoplasmic maturation of the small ribosomal subunit requires RIO proteins in Saccharomyces cerevisiae
    • E. Vanrobays, J.P. Gelugne, P.E. Gleizes, and M. Caizergues-Ferrer Late cytoplasmic maturation of the small ribosomal subunit requires RIO proteins in Saccharomyces cerevisiae Mol. Cell. Biol. 23 2003 2083 2095
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2083-2095
    • Vanrobays, E.1    Gelugne, J.P.2    Gleizes, P.E.3    Caizergues-Ferrer, M.4
  • 42
    • 4444348265 scopus 로고    scopus 로고
    • Crystal structure of A. fulgidus Rio2 defines a new family of serine protein kinases
    • N. LaRonde-LeBlanc, and A. Wlodawer Crystal structure of A. fulgidus Rio2 defines a new family of serine protein kinases Structure 12 2004 1585 1594
    • (2004) Structure , vol.12 , pp. 1585-1594
    • Laronde-Leblanc, N.1    Wlodawer, A.2
  • 44
    • 0037205733 scopus 로고    scopus 로고
    • RIO1, an extraordinary novel protein kinase
    • M. Angermayr, and W. Bandlow RIO1, an extraordinary novel protein kinase FEBS Lett. 524 2002 31 36
    • (2002) FEBS Lett. , vol.524 , pp. 31-36
    • Angermayr, M.1    Bandlow, W.2
  • 45
    • 20444440742 scopus 로고    scopus 로고
    • Autophosphorylation of A. fulgidus Rio2 and crystal structures of its nucleotide-metal ion complexes
    • N. LaRonde-LeBlanc, T. Guszczynski, T.D. Copeland, and A. Wlodawer Autophosphorylation of A. fulgidus Rio2 and crystal structures of its nucleotide-metal ion complexes FEBS J. 272 2005 2800 2810
    • (2005) FEBS J. , vol.272 , pp. 2800-2810
    • Laronde-Leblanc, N.1    Guszczynski, T.2    Copeland, T.D.3    Wlodawer, A.4
  • 48
    • 1842419667 scopus 로고    scopus 로고
    • Structure of the la motif: A winged helix domain mediates RNA binding via a conserved aromatic patch
    • G. Dong, G. Chakshusmathi, S.L. Wolin, and K.M. Reinisch Structure of the La motif: a winged helix domain mediates RNA binding via a conserved aromatic patch EMBO J. 23 2004 1000 1007
    • (2004) EMBO J. , vol.23 , pp. 1000-1007
    • Dong, G.1    Chakshusmathi, G.2    Wolin, S.L.3    Reinisch, K.M.4
  • 49
    • 19244376200 scopus 로고    scopus 로고
    • Isolation of the Aspergillus nidulans sudD gene and its human homologue
    • P. Anaya, S.C. Evans, C. Dai, G. Lozano, and G.S. May Isolation of the Aspergillus nidulans sudD gene and its human homologue Gene 211 1998 323 329
    • (1998) Gene , vol.211 , pp. 323-329
    • Anaya, P.1    Evans, S.C.2    Dai, C.3    Lozano, G.4    May, G.S.5
  • 50
    • 0037363075 scopus 로고    scopus 로고
    • Does the ribosome translate cancer?
    • D. Ruggero, and P.P. Pandolfi Does the ribosome translate cancer? Nat. Rev., Cancer 3 2003 179 192
    • (2003) Nat. Rev., Cancer , vol.3 , pp. 179-192
    • Ruggero, D.1    Pandolfi, P.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.