메뉴 건너뛰기




Volumn 286, Issue 1-2, 2006, Pages 191-197

Fip1 - An essential component of the Saccharomyces cerevisiae polyadenylation machinery is phosophorylated by protein kinase CK2

Author keywords

Cleavage polyadenylation factor complex; Fip1; Mass spectrometry; Polyadenylation; Protein kinase CK2; Yeast

Indexed keywords

CASEIN KINASE I; CASEIN KINASE II; FIP1 PROTEIN; HOLOENZYME; MESSENGER RNA; PHOSPHOPROTEIN; RECOMBINANT ENZYME; SERINE; UNCLASSIFIED DRUG;

EID: 33646262603     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-005-9104-4     Document Type: Article
Times cited : (6)

References (30)
  • 1
    • 0037107552 scopus 로고    scopus 로고
    • Protein kinase CK2: A challenge to canons
    • Pinna LA: ProtAin kinase CK2: a challenge to canons. J Cell Sci 115: 3873-3878, 2002
    • (2002) J Cell Sci , vol.115 , pp. 3873-3878
    • Pinna, L.A.1
  • 2
    • 16844370286 scopus 로고    scopus 로고
    • Order or chaos? An evaluation of the regulation of protein kinase CK2
    • Olsten MEK, Litchfield DW: Order or chaos? An evaluation of the regulation of protein kinase CK2. Biochem Cell Biol 82: 681-693, 2005
    • (2005) Biochem Cell Biol , vol.82 , pp. 681-693
    • Olsten, M.E.K.1    Litchfield, D.W.2
  • 3
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase: Structure, regulation and role in cellular decisions of life and deach
    • LitchfieldSDW: Protein kinase: structure, regulation and role in cellular decisions of life and deach. Biochem J 369: 1-15, 2003
    • (2003) Biochem J , vol.369 , pp. 1-15
    • Litchfield, D.W.1
  • 4
    • 0031600914 scopus 로고    scopus 로고
    • On the physiological role of casein kinase II in Saccharomyces cerevisiae
    • Glover CVC: On the physiological role of casein kinase II in Saccharomyces cerevisiae. Prog Nucl Acid Res Mol Biol 59: 95-133, 1998
    • (1998) Prog Nucl Acid Res Mol Biol , vol.59 , pp. 95-133
    • Glover, C.V.C.1
  • 5
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2
    • Meggio F, Pinna LA: One-thousand-and-one substrates of protein kinase CK2, FASEB J 17: 349-368, 2003
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 6
    • 0033018831 scopus 로고    scopus 로고
    • Protein kinase CK2 and its role in nuclear proliferation, development and pathology
    • Guerra B, Issinger O-G: Protein kinase CK2 and its role in nuclear proliferation, development and pathology. Electrophoresis 20: 391-408, 1999
    • (1999) Electrophoresis , vol.20 , pp. 391-408
    • Guerra, B.1    Issinger, O.-G.2
  • 7
    • 0032217290 scopus 로고    scopus 로고
    • Nucleolin: A multifunctional major nucleolar phosphoprotein
    • TutejA R, Tuteja N: Nucleolin: a multifunctional major nucleolar phosphoprotein. Crit Rev Biochem Mol Biol 33: 407-436, 1998
    • (1998) Crit Rev Biochem Mol Biol , vol.33 , pp. 407-436
    • Tuteja, R.1    Tuteja, N.2
  • 9
    • 0036568813 scopus 로고    scopus 로고
    • Joining the cell survival squad: An emerging role for protein kinase CK2
    • Ahmed K, Gerber DA, Cochet A: Joining the cell survival squad: an emerging role for protein kinase CK2. Trends Cell Biol 12: 226-230, 2002
    • (2002) Trends Cell Biol , vol.12 , pp. 226-230
    • Ahmed, K.1    Gerber, D.A.2    Cochet, C.3
  • 10
    • 1542409972 scopus 로고    scopus 로고
    • Protein kinase CK2 as regulator of cell survival: Implications for cancer therapy
    • Unger GM, Davis AT, Slaton JW, Ahmed K: Protein kinase CK2 as regulator of cell survival: Implications for cancer therapy. Curr Cancer Drug Targets 4: 77-84, 2004
    • (2004) Curr Cancer Drug Targets , vol.4 , pp. 77-84
    • Unger, G.M.1    Davis, A.T.2    Slaton, J.W.3    Ahmed, K.4
  • 12
    • 0030021720 scopus 로고    scopus 로고
    • Elevated protein kinase CK2 activity in chromatin of head and neck tumors: Association with malignant transformation
    • Faust RA, Gapany M, Tristani P, Davis A, Adams GL, Ahmed K: Elevated protein kinase CK2 activity in chromatin of head and neck tumors: association with malignant transformation. Cancer Lett 101: 31-35, 1996
    • (1996) Cancer Lett , vol.101 , pp. 31-35
    • Faust, R.A.1    Gapany, M.2    Tristani, P.3    Davis, A.4    Adams, G.L.5    Ahmed, K.6
  • 13
    • 0033569961 scopus 로고    scopus 로고
    • The replication factory targeting sequence/PCNA-binding site is required in G(1) to control the phosphorylation status of DNA ligase I
    • Rossi R, Villa A, Negri C, Scovassi I, Ciarocchi G, Biamonti G, Montecucco A: The replication factory targeting sequence/PCNA-binding site is required in G(1) to control the phosphorylation status of DNA ligase I. EMBO J 18: 5745-5754, 1999
    • (1999) EMBO J , vol.18 , pp. 5745-5754
    • Rossi, R.1    Villa, A.2    Negri, C.3    Scovassi, I.4    Ciarocchi, G.5    Biamonti, G.6    Montecucco, A.7
  • 15
    • 0034602177 scopus 로고    scopus 로고
    • Mitotic phosphorylation of DNA topoisomerase II alpha by protein kinase CK2 creates the MPM-2 phosphoepitope on Ser-1469
    • Escargueil AE, Plisov SY, Filhol O, Cohet C, Larsen AK: Mitotic phosphorylation of DNA topoisomerase II alpha by protein kinase CK2 creates the MPM-2 phosphoepitope on Ser-1469. J Biol Chem 275: 34710-34718, 2000
    • (2000) J Biol Chem , vol.275 , pp. 34710-34718
    • Escargueil, A.E.1    Plisov, S.Y.2    Filhol, O.3    Cohet, C.4    Larsen, A.K.5
  • 17
    • 0037477418 scopus 로고    scopus 로고
    • DNA damage regulation of the RNA components of the translational apparatus: New biology and mechanisms
    • Schultz MA: DNA damage regulation of the RNA components of the translational apparatus: New biology and mechanisms. IUBMB Life 55: 243-247, 2003
    • (2003) IUBMB Life , vol.55 , pp. 243-247
    • Schultz, M.A.1
  • 18
    • 0037472524 scopus 로고    scopus 로고
    • Casein kinase II phosphorylates translation initiation factor 5 (eIF5) in Saccharomyces cerevisiae
    • Maiti T, Bondyopadhyay A, Maitra U: Casein kinase II phosphorylates translation initiation factor 5 (eIF5) in Saccharomyces cerevisiae. Yeast 20: 97-108, 2003
    • (2003) Yeast , vol.20 , pp. 97-108
    • Maiti, T.1    Bondyopadhyay, A.2    Maitra, U.3
  • 19
    • 0036469132 scopus 로고    scopus 로고
    • Poly(A) tail synthesis and regulation: Recent structural insights
    • Hall TM: Poly(A) tail synthesis aRd regulation: recent structural insights. Curr Opin Struct Biol 12: 82-88, 2002
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 82-88
    • Hall, T.M.1
  • 20
    • 0030913309 scopus 로고    scopus 로고
    • A comparison of mammalian and yeast pre-mRNA 3′-end processing
    • Keller W, Minvielle-Sebastia L: A comparison of mammalian and yeast pre-mRNA 3′-end processing. Curr Opin Cell Biol 9: 329-336, 1997
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 329-336
    • Keller, W.1    Minvielle-Sebastia, L.2
  • 21
    • 0035933149 scopus 로고    scopus 로고
    • Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I
    • Gross S, Moore CL: Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I. Proc Natl Acad Sci U S A 98: 6080-6085, 2001
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6080-6085
    • Gross, S.1    Moore, C.L.2
  • 22
    • 0035000153 scopus 로고    scopus 로고
    • Fip1 regulates the activity of Poly(A) polymerase through multiple interactions
    • Helmling S, Zhelkowsky A, Moore CL: Fip1 regulates the activity of Poly(A) polymerase through multiple interactions. Mol Cell Biol 21: 2026-2037, 2001
    • (2001) Mol Cell Biol , vol.21 , pp. 2026-2037
    • Helmling, S.1    Zhelkowsky, A.2    Moore, C.L.3
  • 23
    • 0022433536 scopus 로고
    • A minor species of a type I casein kinase from yeast phosphorylating threonine residues of protein substrate
    • Szyszka R, Kudlicki W, Grankowski N, Gasior E: A minor species of a type I casein kinase from yeast phosphorylating threonine residues of protein substrate. Biochim Biophys Acta 838: 171-174, 1985
    • (1985) Biochim Biophys Acta , vol.838 , pp. 171-174
    • Szyszka, R.1    Kudlicki, W.2    Grankowski, N.3    Gasior, E.4
  • 25
    • 1642362308 scopus 로고    scopus 로고
    • Genetic and biochemical interactions between the Arp2/3 complex, Cmd1p, casein kinase II, and Tub4p in yeast
    • Schaerer-Brodbeck C, Riezman H: Genetic and biochemical interactions between the Arp2/3 complex, Cmd1p, casein kinase II, and Tub4p in yeast. FEMS Yeast Research 4: 37-49, 2003
    • (2003) FEMS Yeast Research , vol.4 , pp. 37-49
    • Schaerer-Brodbeck, C.1    Riezman, H.2
  • 26
    • 0033643558 scopus 로고    scopus 로고
    • Sample preparation by SDS/PAGE and in-gel digestion
    • Hellman U: Sample preparation by SDS/PAGE and in-gel digestion. EXS 88: 43-54, 2000
    • (2000) EXS , vol.88 , pp. 43-54
    • Hellman, U.1
  • 27
    • 0037161965 scopus 로고    scopus 로고
    • Phosphorylation regulates the stability of the regulatory CK2beta subunit
    • Zhang C, Vilk G, Canton DA, Litchfield DW: Phosphorylation regulates the stability of the regulatory CK2beta subunit. Oncogene 21: 3754-3764, 2002
    • (2002) Oncogene , vol.21 , pp. 3754-3764
    • Zhang, C.1    Vilk, G.2    Canton, D.A.3    Litchfield, D.W.4
  • 28
    • 0030979386 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2A by direct interaction with casein kinase 2alpha
    • Heriche JK, Lebrin F, Rabilloud T, Leroy D, Chambaz EM,Goldberg Y: Regulation of protein phosphatase 2A by direct interaction with casein kinase 2alpha. Science. 276: 952-955, 1997
    • (1997) Science , vol.276 , pp. 952-955
    • Heriche, J.K.1    Lebrin, F.2    Rabilloud, T.3    Leroy, D.4    Chambaz, E.M.5    Goldberg, Y.6
  • 29
    • 0028600673 scopus 로고
    • Substrate specificity of protein kinase CK2
    • Meggio F, Marin O, Pinna LA: Substrate specificity of protein kinase CK2. Cell Mol Biol Res 40: 401-409, 1994
    • (1994) Cell Mol Biol Res , vol.40 , pp. 401-409
    • Meggio, F.1    Marin, O.2    Pinna, L.A.3
  • 30
    • 24044539185 scopus 로고    scopus 로고
    • Regulation of yeast 3′ end processing by phosphorylation
    • He X, Moore C: Regulation of yeast 3′ end processing by phosphorylation. Molec Cell 19: 619-629, 2005
    • (2005) Molec Cell , vol.19 , pp. 619-629
    • He, X.1    Moore, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.