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Volumn 110, Issue 26, 2013, Pages 10574-10579

Crystal structure of the Golgi casein kinase

Author keywords

Amelogenesis imperfecta; Enamel renal syndrome; Fam20A; Fam20B; Hypophosphatemia

Indexed keywords

ADENOSINE DIPHOSPHATE; CAENORHABDITIS ELEGANS PROTEIN; CASEIN KINASE; DISULFIDE; FAM20C PROTEIN; MANGANESE; NUCLEOTIDE; PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 84879520492     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1309211110     Document Type: Article
Times cited : (63)

References (44)
  • 1
    • 0036097364 scopus 로고    scopus 로고
    • The origins of protein phosphorylation
    • Cohen P (2002) The origins of protein phosphorylation. Nat Cell Biol 4(5): E127-E130.
    • (2002) Nat Cell Biol , vol.4 , Issue.5
    • Cohen, P.1
  • 2
    • 84872321691 scopus 로고    scopus 로고
    • Cellular regulation by protein phosphorylation
    • Fischer EH (2013) Cellular regulation by protein phosphorylation. Biochem Biophys Res Commun 430(2):865-867.
    • (2013) Biochem Biophys Res Commun , vol.430 , Issue.2 , pp. 865-867
    • Fischer, E.H.1
  • 3
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: Evolution of dynamic regulatory proteins
    • Taylor SS, Kornev AP (2011) Protein kinases: Evolution of dynamic regulatory proteins. Trends Biochem Sci 36(2):65-77.
    • (2011) Trends Biochem Sci , vol.36 , Issue.2 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 4
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M, Kuriyan J (2002) The conformational plasticity of protein kinases. Cell 109(3): 275-282.
    • (2002) Cell , vol.109 , Issue.3 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 5
    • 84861859600 scopus 로고    scopus 로고
    • The structural basis for control of eukaryotic protein kinases
    • Endicott JA, Noble ME, Johnson LN (2012) The structural basis for control of eukaryotic protein kinases. Annu Rev Biochem 81:587-613.
    • (2012) Annu Rev Biochem , vol.81 , pp. 587-613
    • Endicott, J.A.1    Noble, M.E.2    Johnson, L.N.3
  • 6
    • 0343910461 scopus 로고
    • Zur frage ob caseín ein einheitlicher stoff sei
    • Hammarsten O (1883) Zur frage ob caseín ein einheitlicher stoff sei. Zeitschrift Physiol Chemie 7:227-273.
    • (1883) Zeitschrift Physiol Chemie , vol.7 , pp. 227-273
    • Hammarsten, O.1
  • 7
    • 84861658918 scopus 로고    scopus 로고
    • Secreted kinase phosphorylates extracellular proteins that regulate biomineralization
    • Tagliabracci VS, et al. (2012) Secreted kinase phosphorylates extracellular proteins that regulate biomineralization. Science 336(6085):1150-1153.
    • (2012) Science , vol.336 , Issue.6085 , pp. 1150-1153
    • Tagliabracci, V.S.1
  • 9
    • 84864713987 scopus 로고    scopus 로고
    • Inhibition of protein kinase CK2 by flavonoids and tyrphostins: A structural insight
    • Lolli G, et al. (2012) Inhibition of protein kinase CK2 by flavonoids and tyrphostins: A structural insight. Biochemistry 51(31):6097-6107.
    • (2012) Biochemistry , vol.51 , Issue.31 , pp. 6097-6107
    • Lolli, G.1
  • 10
    • 84865021971 scopus 로고    scopus 로고
    • The Raine syndrome protein FAM20C is a Golgi kinase that phosphorylates bio-mineralization proteins
    • Ishikawa HO, Xu A, Ogura E, Manning G, Irvine KD (2012) The Raine syndrome protein FAM20C is a Golgi kinase that phosphorylates bio-mineralization proteins. PLoS ONE 7(8):e42988.
    • (2012) PLoS ONE , vol.7 , Issue.8
    • Ishikawa, H.O.1    Xu, A.2    Ogura, E.3    Manning, G.4    Irvine, K.D.5
  • 11
    • 50049110046 scopus 로고    scopus 로고
    • Characterization of the human cerebrospinal fluid phosphoproteome by titanium dioxide affinity chromatography and mass spectrometry
    • Bahl JM, Jensen SS, Larsen MR, Heegaard NH (2008) Characterization of the human cerebrospinal fluid phosphoproteome by titanium dioxide affinity chromatography and mass spectrometry. Anal Chem 80(16):6308-6316.
    • (2008) Anal Chem , vol.80 , Issue.16 , pp. 6308-6316
    • Bahl, J.M.1    Jensen, S.S.2    Larsen, M.R.3    Heegaard, N.H.4
  • 12
    • 71549137428 scopus 로고    scopus 로고
    • An initial characterization of the serum phosphoproteome
    • Zhou W, et al. (2009) An initial characterization of the serum phosphoproteome. J Proteome Res 8(12):5523-5531.
    • (2009) J Proteome Res , vol.8 , Issue.12 , pp. 5523-5531
    • Zhou, W.1
  • 13
    • 77954594787 scopus 로고    scopus 로고
    • Motif analysis of phosphosites discloses a potential prominent role of the Golgi casein kinase (GCK) in the generation of human plasma phospho-proteome
    • Salvi M, Cesaro L, Tibaldi E, Pinna LA (2010) Motif analysis of phosphosites discloses a potential prominent role of the Golgi casein kinase (GCK) in the generation of human plasma phospho-proteome. J Proteome Res 9(6):3335-3338.
    • (2010) J Proteome Res , vol.9 , Issue.6 , pp. 3335-3338
    • Salvi, M.1    Cesaro, L.2    Tibaldi, E.3    Pinna, L.A.4
  • 14
    • 0024306493 scopus 로고
    • Unknown syndrome: Microcephaly, hypoplastic nose, exophthalmos, gum hyperplasia, cleft palate, low-set ears, and osteosclerosis
    • Raine J, Winter RM, Davey A, Tucker SM (1989) Unknown syndrome: Microcephaly, hypoplastic nose, exophthalmos, gum hyperplasia, cleft palate, low-set ears, and osteosclerosis. J Med Genet 26(12):786-788.
    • (1989) J Med Genet , vol.26 , Issue.12 , pp. 786-788
    • Raine, J.1    Winter, R.M.2    Davey, A.3    Tucker, S.M.4
  • 15
    • 35348873113 scopus 로고    scopus 로고
    • Mutations in FAM20C are associated with lethal osteosclerotic bone dysplasia (Raine syndrome), highlighting a crucial molecule in bone development
    • Simpson MA, et al. (2007) Mutations in FAM20C are associated with lethal osteosclerotic bone dysplasia (Raine syndrome), highlighting a crucial molecule in bone development. Am J Hum Genet 81(5):906-912.
    • (2007) Am J Hum Genet , vol.81 , Issue.5 , pp. 906-912
    • Simpson, M.A.1
  • 16
    • 79960283233 scopus 로고    scopus 로고
    • Osteosclerotic bone dysplasia in siblings with a Fam20C mutation
    • Fradin M, et al. (2011) Osteosclerotic bone dysplasia in siblings with a Fam20C mutation. Clin Genet 80(2):177-183.
    • (2011) Clin Genet , vol.80 , Issue.2 , pp. 177-183
    • Fradin, M.1
  • 17
    • 60549093755 scopus 로고    scopus 로고
    • Mutations in FAM20C also identified in non-lethal osteosclerotic bone dysplasia
    • Simpson MA, et al. (2009) Mutations in FAM20C also identified in non-lethal osteosclerotic bone dysplasia. Clin Genet 75(3):271-276.
    • (2009) Clin Genet , vol.75 , Issue.3 , pp. 271-276
    • Simpson, M.A.1
  • 18
    • 84878219688 scopus 로고    scopus 로고
    • Exome sequencing reveals FAM20c mutations associated with FGF23-related hypophosphatemia, dental anomalies and ectopic calcification
    • Rafaelsen SH, et al. (2013) Exome sequencing reveals FAM20c mutations associated with FGF23-related hypophosphatemia, dental anomalies and ectopic calcification. J Bone Miner Res 28(6):1378-1385.
    • (2013) J Bone Miner Res , vol.28 , Issue.6 , pp. 1378-1385
    • Rafaelsen, S.H.1
  • 19
    • 84868686755 scopus 로고    scopus 로고
    • Amelogenesis imperfecta and other biomineralization defects in Fam20a and Fam20c null mice
    • Vogel P, et al. (2012) Amelogenesis imperfecta and other biomineralization defects in Fam20a and Fam20c null mice. Vet Pathol 49(6):998-1017.
    • (2012) Vet Pathol , vol.49 , Issue.6 , pp. 998-1017
    • Vogel, P.1
  • 20
    • 84863698813 scopus 로고    scopus 로고
    • Inactivation of a novel FGF23 regulator, FAM20C, leads to hypophosphatemic rickets in mice
    • Wang X, et al. (2012) Inactivation of a novel FGF23 regulator, FAM20C, leads to hypophosphatemic rickets in mice. PLoS Genet 8(5):e1002708.
    • (2012) PLoS Genet , vol.8 , Issue.5
    • Wang, X.1
  • 21
    • 84867777177 scopus 로고    scopus 로고
    • FAM20C plays an essential role in the formation of murine teeth
    • Wang X, et al. (2012) FAM20C plays an essential role in the formation of murine teeth. J Biol Chem 287(43):35934-35942.
    • (2012) J Biol Chem , vol.287 , Issue.43 , pp. 35934-35942
    • Wang, X.1
  • 22
    • 25444456098 scopus 로고    scopus 로고
    • FAM20: An evolutionarily conserved family of secreted proteins expressed in hematopoietic cells
    • Nalbant D, et al. (2005) FAM20: An evolutionarily conserved family of secreted proteins expressed in hematopoietic cells. BMC Genomics 6:11.
    • (2005) BMC Genomics , vol.6 , pp. 11
    • Nalbant, D.1
  • 23
    • 67651027850 scopus 로고    scopus 로고
    • FAM20B is a kinase that phosphorylates xylose in the glycosaminoglycan- protein linkage region
    • Koike T, Izumikawa T, Tamura J, Kitagawa H (2009) FAM20B is a kinase that phosphorylates xylose in the glycosaminoglycan-protein linkage region. Biochem J 421(2): 157-162.
    • (2009) Biochem J , vol.421 , Issue.2 , pp. 157-162
    • Koike, T.1    Izumikawa, T.2    Tamura, J.3    Kitagawa, H.4
  • 24
    • 84875969039 scopus 로고    scopus 로고
    • EXTL2, a member of the EXT family of tumor suppressors, controls glycosaminoglycan biosynthesis in a xylose kinase-dependent manner
    • Nadanaka S, et al. (2013) EXTL2, a member of the EXT family of tumor suppressors, controls glycosaminoglycan biosynthesis in a xylose kinase-dependent manner. J Biol Chem 288(13):9321-9333.
    • (2013) J Biol Chem , vol.288 , Issue.13 , pp. 9321-9333
    • Nadanaka, S.1
  • 25
    • 80052327147 scopus 로고    scopus 로고
    • Mutations in fam20b and xylt1 reveal that cartilage matrix controls timing of endochondral ossification by inhibiting chondrocyte maturation
    • Eames BF, et al. (2011) Mutations in fam20b and xylt1 reveal that cartilage matrix controls timing of endochondral ossification by inhibiting chondrocyte maturation. PLoS Genet 7(8):e1002246.
    • (2011) PLoS Genet , vol.7 , Issue.8
    • Eames, B.F.1
  • 26
    • 79955836955 scopus 로고    scopus 로고
    • Whole-exome sequencing identifies FAM20A mutations as a cause of amelogenesis imperfecta and gingival hyperplasia syndrome
    • O'Sullivan J, et al. (2011) Whole-exome sequencing identifies FAM20A mutations as a cause of amelogenesis imperfecta and gingival hyperplasia syndrome. Am J Hum Genet 88(5):616-620.
    • (2011) Am J Hum Genet , vol.88 , Issue.5 , pp. 616-620
    • O'Sullivan, J.1
  • 27
    • 84857691762 scopus 로고    scopus 로고
    • Novel FAM20A mutations in hypoplastic amelogenesis imperfecta
    • Cho SH, et al. (2012) Novel FAM20A mutations in hypoplastic amelogenesis imperfecta. Hum Mutat 33(1):91-94.
    • (2012) Hum Mutat , vol.33 , Issue.1 , pp. 91-94
    • Cho, S.H.1
  • 28
    • 84876377978 scopus 로고    scopus 로고
    • Nephrocalcinosis (enamel renal syndrome) caused by autosomal recessive FAM20A mutations
    • Jaureguiberry G, et al. (2012) Nephrocalcinosis (enamel renal syndrome) caused by autosomal recessive FAM20A mutations. Nephron, Physiol 122(1-2):1-6.
    • (2012) Nephron, Physiol , vol.122 , Issue.1-2 , pp. 1-6
    • Jaureguiberry, G.1
  • 29
    • 84874098001 scopus 로고    scopus 로고
    • FAM20A mutations can cause enamel-renal syndrome (ERS)
    • Wang SK, et al. (2013) FAM20A mutations can cause enamel-renal syndrome (ERS). PLoS Genet 9(2):e1003302.
    • (2013) PLoS Genet , vol.9 , Issue.2
    • Wang, S.K.1
  • 30
    • 33644788720 scopus 로고    scopus 로고
    • Genes and related proteins involved in amelogenesis imperfecta
    • Stephanopoulos G, Garefalaki ME, Lyroudia K (2005) Genes and related proteins involved in amelogenesis imperfecta. J Dent Res 84(12):1117-1126.
    • (2005) J Dent Res , vol.84 , Issue.12 , pp. 1117-1126
    • Stephanopoulos, G.1    Garefalaki, M.E.2    Lyroudia, K.3
  • 31
    • 0021929841 scopus 로고
    • Syndrome of amelogenesis imperfecta, nephrocalcinosis, impaired renal concentration, and possible abnormality of calcium metabolism
    • Lubinsky M, Angle C, Marsh PW, Witkop CJ, Jr. (1985) Syndrome of amelogenesis imperfecta, nephrocalcinosis, impaired renal concentration, and possible abnormality of calcium metabolism. Am J Med Genet 20(2):233-243.
    • (1985) Am J Med Genet , vol.20 , Issue.2 , pp. 233-243
    • Lubinsky, M.1    Angle, C.2    Marsh, P.W.3    Witkop Jr., C.J.4
  • 32
    • 41849110846 scopus 로고    scopus 로고
    • Structural evolution of the protein kinase-like superfamily
    • Scheeff ED, Bourne PE (2005) Structural evolution of the protein kinase-like superfamily. PLOS Comput Biol 1(5):e49.
    • (2005) PLOS Comput Biol , vol.1 , Issue.5
    • Scheeff, E.D.1    Bourne, P.E.2
  • 33
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm L, Rosenstrom P (2010) Dali server: Conservation mapping in 3D. Nucleic Acids Res 38(Web Server issue):W545-W549.
    • (2010) Nucleic Acids Res , vol.38 , Issue.WEB SERVER ISSUE
    • Holm, L.1    Rosenstrom, P.2
  • 34
    • 0042357069 scopus 로고    scopus 로고
    • The functional glycosyltransferase signature sequence of the human beta 1,3-glucuronosyltransferase is a XDD motif
    • Gulberti S, et al. (2003) The functional glycosyltransferase signature sequence of the human beta 1,3-glucuronosyltransferase is a XDD motif. J Biol Chem 278(34): 32219-32226.
    • (2003) J Biol Chem , vol.278 , Issue.34 , pp. 32219-32226
    • Gulberti, S.1
  • 35
    • 58449087611 scopus 로고    scopus 로고
    • Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB
    • Schumacher MA, et al. (2009) Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB. Science 323(5912):396-401.
    • (2009) Science , vol.323 , Issue.5912 , pp. 396-401
    • Schumacher, M.A.1
  • 36
    • 78650750316 scopus 로고    scopus 로고
    • Helicobacter pylori proinflammatory protein up-regulates NFkappaB as a cell-translocating Ser/Thr kinase
    • Kim J, et al. (2010) Helicobacter pylori proinflammatory protein up-regulates NFkappaB as a cell-translocating Ser/Thr kinase. Proc Natl Acad Sci USA 107(50): 21418-21423.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.50 , pp. 21418-21423
    • Kim, J.1
  • 37
    • 79959476700 scopus 로고    scopus 로고
    • The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling
    • Dar AC, Shokat KM (2011) The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling. Annu Rev Biochem 80:769-795.
    • (2011) Annu Rev Biochem , vol.80 , pp. 769-795
    • Dar, A.C.1    Shokat, K.M.2
  • 38
    • 0034699382 scopus 로고    scopus 로고
    • A chemical switch for inhibitor-sensitive alleles of any protein kinase
    • Bishop AC, et al. (2000) A chemical switch for inhibitor-sensitive alleles of any protein kinase. Nature 407(6802):395-401.
    • (2000) Nature , vol.407 , Issue.6802 , pp. 395-401
    • Bishop, A.C.1
  • 39
    • 0031019426 scopus 로고    scopus 로고
    • Rat liver Golgi apparatus contains a protein kinase similar to the casein kinase of lactating mammary gland
    • Lasa M, Marin O, Pinna LA (1997) Rat liver Golgi apparatus contains a protein kinase similar to the casein kinase of lactating mammary gland. Eur J Biochem 243(3): 719-725.
    • (1997) Eur J Biochem , vol.243 , Issue.3 , pp. 719-725
    • Lasa, M.1    Marin, O.2    Pinna, L.A.3
  • 40
    • 0034332613 scopus 로고    scopus 로고
    • Novel consensus sequence for the Golgi apparatus casein kinase, revealed using proline-rich protein-1 (PRP1)-derived peptide substrates
    • Brunati AM, Marin O, Bisinella A, Salviati A, Pinna LA (2000) Novel consensus sequence for the Golgi apparatus casein kinase, revealed using proline-rich protein-1 (PRP1)-derived peptide substrates. Biochem J 351(Pt 3):765-768.
    • (2000) Biochem J , vol.351 , Issue.PART 3 , pp. 765-768
    • Brunati, A.M.1    Marin, O.2    Bisinella, A.3    Salviati, A.4    Pinna, L.A.5
  • 41
    • 33845197964 scopus 로고    scopus 로고
    • Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism
    • Kornev AP, Haste NM, Taylor SS, Eyck LF (2006) Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism. Proc Natl Acad Sci USA 103(47):17783-17788.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.47 , pp. 17783-17788
    • Kornev, A.P.1    Haste, N.M.2    Taylor, S.S.3    Eyck, L.F.4
  • 42
    • 0033152604 scopus 로고    scopus 로고
    • The crystal structure of the Physarum polycephalum actinfragmin kinase: An atypical protein kinase with a specialized substrate-binding domain
    • Steinbacher S, et al. (1999) The crystal structure of the Physarum polycephalum actinfragmin kinase: An atypical protein kinase with a specialized substrate-binding domain. EMBO J 18(11):2923-2929.
    • (1999) EMBO J , vol.18 , Issue.11 , pp. 2923-2929
    • Steinbacher, S.1
  • 43
    • 75349091799 scopus 로고    scopus 로고
    • Defining the conserved internal architecture of a protein kinase
    • Kornev AP, Taylor SS (2010) Defining the conserved internal architecture of a protein kinase. Biochim Biophys Acta 1804(3):440-444.
    • (2010) Biochim Biophys Acta , vol.1804 , Issue.3 , pp. 440-444
    • Kornev, A.P.1    Taylor, S.S.2


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