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Volumn 41, Issue 4, 2013, Pages 1061-1065

Phosphorylation of substrates destined for secretion by the Fam20 kinases

Author keywords

Amelogenesis imperfecta; Fam20A; Fam20B; Fam20C; Hypophosphataemia; Raine syndrome

Indexed keywords

PHOSPHATE; PHOSPHOPROTEIN; PROTEIN FAM20; PROTEIN KINASE; PROTEOGLYCAN; UNCLASSIFIED DRUG;

EID: 84880516022     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20130059     Document Type: Article
Times cited : (21)

References (49)
  • 1
    • 0036097364 scopus 로고    scopus 로고
    • The origins of protein phosphorylation
    • Cohen, P. (2002) The origins of protein phosphorylation. Nat. Cell Biol. 4, E127-E130
    • (2002) Nat. Cell Biol. , vol.4
    • Cohen, P.1
  • 3
    • 50049110046 scopus 로고    scopus 로고
    • Characterization of the human cerebrospinal fluid phosphoproteome by titanium dioxide affinity chromatography and mass spectrometry
    • Bahl, J.M., Jensen, S.S., Larsen, M.R. and Heegaard, N.H. (2008) Characterization of the human cerebrospinal fluid phosphoproteome by titanium dioxide affinity chromatography and mass spectrometry. Anal. Chem. 80, 6308-6316
    • (2008) Anal. Chem. , vol.80 , pp. 6308-6316
    • Bahl, J.M.1    Jensen, S.S.2    Larsen, M.R.3    Heegaard, N.H.4
  • 5
    • 84871504913 scopus 로고    scopus 로고
    • Extracellular phosphorylation and phosphorylated proteins: Not just curiosities but physiologically important
    • Yalak, G. and Vogel, V. (2012) Extracellular phosphorylation and phosphorylated proteins: not just curiosities but physiologically important. Sci. Signaling 5, re7
    • (2012) Sci. Signaling , vol.5
    • Yalak, G.1    Vogel, V.2
  • 6
    • 0019400281 scopus 로고
    • Phosphorylation of caseins, present evidence for an amino acid triplet code posttranslationally recognized by specific kinases
    • Mercier, J.C. (1981) Phosphorylation of caseins, present evidence for an amino acid triplet code posttranslationally recognized by specific kinases. Biochimie 63, 1-17
    • (1981) Biochimie , vol.63 , pp. 1-17
    • Mercier, J.C.1
  • 7
    • 0343910461 scopus 로고
    • Zur Frage ob das Caseïn ein einheitlicher Stoff sei
    • Hammarsten, O. (1883) Zur Frage ob das Caseïn ein einheitlicher Stoff sei. Z. Physiol. Chem. 7, 227-273
    • (1883) Z. Physiol. Chem. , vol.7 , pp. 227-273
    • Hammarsten, O.1
  • 8
    • 0001010573 scopus 로고
    • The enzymatic phosphorylation of proteins
    • Burnett, G. and Kennedy, E.P. (1954) The enzymatic phosphorylation of proteins. J. Biol. Chem. 211, 969-980
    • (1954) J. Biol. Chem. , vol.211 , pp. 969-980
    • Burnett, G.1    Kennedy, E.P.2
  • 9
    • 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. and Pinna, L.A. (1997) Rat liver Golgi apparatus contains a protein kinase similar to the casein kinase of lactating mammary gland. Eur. J. Biochem. 243, 719-725
    • (1997) Eur. J. Biochem. , vol.243 , pp. 719-725
    • Lasa, M.1    Marin, O.2    Pinna, L.A.3
  • 10
    • 0029937923 scopus 로고    scopus 로고
    • Golgi apparatus mammary gland casein kinase: Monitoring by a specific peptide substrate and definition of specificity determinants
    • Lasa-Benito, M., Marin, O., Meggio, F. and Pinna, L.A. (1996) Golgi apparatus mammary gland casein kinase: monitoring by a specific peptide substrate and definition of specificity determinants. FEBS Lett. 382, 149-152
    • (1996) FEBS Lett. , vol.382 , pp. 149-152
    • Lasa-Benito, M.1    Marin, O.2    Meggio, F.3    Pinna, L.A.4
  • 11
    • 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. and Pinna, L.A. (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, 3335-3338
    • (2010) J. Proteome Res. , vol.9 , pp. 3335-3338
    • Salvi, M.1    Cesaro, L.2    Tibaldi, E.3    Pinna, L.A.4
  • 12
    • 0034283572 scopus 로고    scopus 로고
    • Purification of Golgi casein kinase from bovine milk
    • Duncan, J.S., Wilkinson, M.C. and Burgoyne, R.D. (2000) Purification of Golgi casein kinase from bovine milk. Biochem. J. 350, 463-468
    • (2000) Biochem. J. , vol.350 , pp. 463-468
    • Duncan, J.S.1    Wilkinson, M.C.2    Burgoyne, R.D.3
  • 13
    • 0015524214 scopus 로고
    • Phosphorylation of casein: Role of the Golgi apparatus
    • Bingham, E.W., Farrell, Jr, H.M. and Basch, J.J. (1972) Phosphorylation of casein: role of the Golgi apparatus. J. Biol. Chem. 247, 8193-8194
    • (1972) J. Biol. Chem. , vol.247 , pp. 8193-8194
    • Bingham, E.W.1    Farrell Jr., H.M.2    Basch, J.J.3
  • 14
    • 0022404862 scopus 로고
    • Purification and tissue-specific expression of casein kinase from the lactating guinea-pig mammary gland
    • Moore, A., Boulton, A.P., Heid, H.W., Jarasch, E.D. and Craig, R.K. (1985) Purification and tissue-specific expression of casein kinase from the lactating guinea-pig mammary gland. Eur. J. Biochem. 152, 729-737
    • (1985) Eur. J. Biochem. , vol.152 , pp. 729-737
    • Moore, A.1    Boulton, A.P.2    Heid, H.W.3    Jarasch, E.D.4    Craig, R.K.5
  • 15
    • 0019616899 scopus 로고
    • Characterisation of a membrane-bound serine-specific casein kinase isolated from lactating guinea-pig mammary gland
    • Pascall, J.C., Boulton, A.P. and Craig, R.K. (1981) Characterisation of a membrane-bound serine-specific casein kinase isolated from lactating guinea-pig mammary gland. Eur. J. Biochem. 119, 91-99
    • (1981) Eur. J. Biochem. , vol.119 , pp. 91-99
    • Pascall, J.C.1    Boulton, A.P.2    Craig, R.K.3
  • 16
    • 47749093500 scopus 로고    scopus 로고
    • Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin domains
    • Ishikawa, H.O., Takeuchi, H., Haltiwanger, R.S. and Irvine, K.D. (2008) Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin domains. Science 321, 401-404
    • (2008) Science , vol.321 , pp. 401-404
    • Ishikawa, H.O.1    Takeuchi, H.2    Haltiwanger, R.S.3    Irvine, K.D.4
  • 18
    • 67651027850 scopus 로고    scopus 로고
    • FAM20B is a kinase that phosphorylates xylose in the glycosaminoglycan- protein linkage region
    • Koike, T., Izumikawa, T., Tamura, J. and Kitagawa, H. (2009) FAM20B is a kinase that phosphorylates xylose in the glycosaminoglycan-protein linkage region. Biochem. J. 421, 157-162
    • (2009) Biochem. J. , vol.421 , pp. 157-162
    • Koike, T.1    Izumikawa, T.2    Tamura, J.3    Kitagawa, H.4
  • 20
    • 84865021971 scopus 로고    scopus 로고
    • The Raine syndrome protein FAM20C is a Golgi kinase that phosphorylates bio-mineralization proteins
    • Ishikawa, H.O., Xu, A., Ogura, E., Manning, G. and Irvine, K.D. (2012) The Raine syndrome protein FAM20C is a Golgi kinase that phosphorylates bio-mineralization proteins. PLoS ONE 7, e42988
    • (2012) PLoS ONE , vol.7
    • Ishikawa, H.O.1    Xu, A.2    Ogura, E.3    Manning, G.4    Irvine, K.D.5
  • 21
    • 0029020282 scopus 로고
    • Protein kinases 6: The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S.K. and Hunter, T. (1995) Protein kinases 6: the eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 22
    • 84878219688 scopus 로고    scopus 로고
    • Exome sequencing reveals FAM20c mutations associated with FGF23-related hypophosphatemia, dental anomalies and ectopic calcification
    • Rafaelsen, S.H., Raeder, H., Fagerheim, A.K., Knappskog, P., Carpenter, T.O., Johansson, S. and Bjerknes, R. (2013) Exome sequencing reveals FAM20c mutations associated with FGF23-related hypophosphatemia, dental anomalies and ectopic calcification. J. Bone Miner. Res. 28, 1378-1385
    • (2013) J. Bone Miner. Res. , vol.28 , pp. 1378-1385
    • Rafaelsen, S.H.1    Raeder, H.2    Fagerheim, A.K.3    Knappskog, P.4    Carpenter, T.O.5    Johansson, S.6    Bjerknes, R.7
  • 23
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D.R., Zheng, J.H., Ten Eyck, L.F., Ashford, V.A., Xuong, N.H., Taylor, S.S. and Sowadski, J.M. (1991) Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-414
    • (1991) Science , vol.253 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 24
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D.R., Zheng, J.H., Ten Eyck, L.F., Xuong, N.H., Taylor, S.S. and Sowadski, J.M. (1991) Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 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
  • 25
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: Evolution of dynamic regulatory proteins
    • Taylor, S.S. and Kornev, A.P. (2011) Protein kinases: evolution of dynamic regulatory proteins. Trends Biochem. Sci. 36, 65-77
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 29
    • 0037200168 scopus 로고    scopus 로고
    • Determination of the glycosaminoglycan-protein linkage region oligosaccharide structures of proteoglycans from Drosophila melanogaster and Caenorhabditis elegans
    • Yamada, S., Okada, Y., Ueno, M., Iwata, S., Deepa, S.S., Nishimura, S., Fujita, M., Van Die, I., Hirabayashi, Y. and Sugahara, K. (2002) Determination of the glycosaminoglycan-protein linkage region oligosaccharide structures of proteoglycans from Drosophila melanogaster and Caenorhabditis elegans. J. Biol. Chem. 277, 31877-31886
    • (2002) J. Biol. Chem. , vol.277 , pp. 31877-31886
    • Yamada, S.1    Okada, Y.2    Ueno, M.3    Iwata, S.4    Deepa, S.S.5    Nishimura, S.6    Fujita, M.7    Van Die, I.8    Hirabayashi, Y.9    Sugahara, K.10
  • 30
    • 0027421906 scopus 로고
    • The Caenorhabditis elegans homologue of the extracellular calcium binding protein SPARC/osteonectin affects nematode body morphology and mobility
    • Schwarzbauer, J.E. and Spencer, C.S. (1993) The Caenorhabditis elegans homologue of the extracellular calcium binding protein SPARC/osteonectin affects nematode body morphology and mobility. Mol. Biol. Cell 4, 941-952
    • (1993) Mol. Biol. Cell , vol.4 , pp. 941-952
    • Schwarzbauer, J.E.1    Spencer, C.S.2
  • 36
    • 0024306493 scopus 로고
    • Unknown syndrome: Microcephaly, hypoplastic nose, exophthalmos, gum hyperplasia, cleft palate, low set ears, and osteosclerosis
    • Raine, J., Winter, R.M., Davey, A. and Tucker, S.M. (1989) Unknown syndrome: microcephaly, hypoplastic nose, exophthalmos, gum hyperplasia, cleft palate, low set ears, and osteosclerosis. J. Med. Genet. 26, 786-788
    • (1989) J. Med. Genet. , vol.26 , pp. 786-788
    • Raine, J.1    Winter, R.M.2    Davey, A.3    Tucker, S.M.4
  • 38
    • 57349158632 scopus 로고    scopus 로고
    • Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition
    • George, A. and Veis, A. (2008) Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition. Chem. Rev. 108, 4670-4693
    • (2008) Chem. Rev. , vol.108 , pp. 4670-4693
    • George, A.1    Veis, A.2
  • 39
  • 42
    • 33750454816 scopus 로고    scopus 로고
    • Loss of DMP1 causes rickets and osteomalacia and identifies a role for osteocytes in mineral metabolism
    • Feng, J.Q., Ward, L.M., Liu, S., Lu, Y., Xie, Y., Yuan, B., Yu, X., Rauch, F., Davis, S.I., Zhang, S. et al. (2006) Loss of DMP1 causes rickets and osteomalacia and identifies a role for osteocytes in mineral metabolism. Nat. Genet. 38, 1310-1315
    • (2006) Nat. Genet. , vol.38 , pp. 1310-1315
    • Feng, J.Q.1    Ward, L.M.2    Liu, S.3    Lu, Y.4    Xie, Y.5    Yuan, B.6    Yu, X.7    Rauch, F.8    Davis, S.I.9    Zhang, S.10
  • 45
    • 33644788720 scopus 로고    scopus 로고
    • Genes and related proteins involved in amelogenesis imperfecta
    • Stephanopoulos, G., Garefalaki, M.E. and Lyroudia, K. (2005) Genes and related proteins involved in amelogenesis imperfecta. J. Dent. Res. 84, 1117-1126
    • (2005) J. Dent. Res. , vol.84 , pp. 1117-1126
    • Stephanopoulos, G.1    Garefalaki, M.E.2    Lyroudia, K.3
  • 46
    • 80052327147 scopus 로고    scopus 로고
    • Mutations in fam20b and xylt1 reveal that cartilage matrix controls timing of endochondral ossification by inhibiting chondrocyte maturation
    • Eames, B.F., Yan, Y.L., Swartz, M.E., Levic, D.S., Knapik, E.W., Postlethwait, J.H. and Kimmel, C.B. (2011) Mutations in fam20b and xylt1 reveal that cartilage matrix controls timing of endochondral ossification by inhibiting chondrocyte maturation. PLoS Genet. 7, e1002246
    • (2011) PLoS Genet. , vol.7
    • Eames, B.F.1    Yan, Y.L.2    Swartz, M.E.3    Levic, D.S.4    Knapik, E.W.5    Postlethwait, J.H.6    Kimmel, C.B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.