메뉴 건너뛰기




Volumn 111, Issue 44, 2014, Pages 15723-15728

Xylose phosphorylation functions as a molecular switch to regulate proteoglycan biosynthesis

Author keywords

Fam20B; GalT II; Proteoglycan; Secretory kinase; Xylose phosphorylation

Indexed keywords

ENZYME; GALACTOSYLTRANSFERASE; GLYCOSAMINOGLYCAN; PHOSPHOTRANSFERASE; PROTEOGLYCAN; SIALIC ACID; TETRASACCHARIDE; XYLOSE; B3GALT6 PROTEIN, HUMAN; SIALIC ACID DERIVATIVE;

EID: 84914689918     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1417993111     Document Type: Article
Times cited : (92)

References (48)
  • 2
    • 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 , pp. E127-E130
    • Cohen, P.1
  • 3
    • 84861567168 scopus 로고    scopus 로고
    • O-linked N,N′-diacetyllactosamine (LacdiNAc)-modified glycans in extracellular matrix glycoproteins are specifically phosphorylated at subterminal N-acetylglucosamine
    • Breloy I, et al. (2012) O-linked N,N′-diacetyllactosamine (LacdiNAc)-modified glycans in extracellular matrix glycoproteins are specifically phosphorylated at subterminal N-acetylglucosamine. J Biol Chem 287(22):18275-18286.
    • (2012) J Biol Chem , vol.287 , Issue.22 , pp. 18275-18286
    • Breloy, I.1
  • 4
    • 0022379159 scopus 로고
    • Structure of the heparan sulfate-protein linkage region. Demonstration of the sequence galactosyl-galactosyl-xylose-2-phosphate
    • Fransson LA, Silverberg I, Carlstedt I (1985) Structure of the heparan sulfate-protein linkage region. Demonstration of the sequence galactosyl-galactosyl-xylose-2-phosphate. J Biol Chem 260(27):14722-14726.
    • (1985) J Biol Chem , vol.260 , Issue.27 , pp. 14722-14726
    • Fransson, L.A.1    Silverberg, I.2    Carlstedt, I.3
  • 5
    • 84882923644 scopus 로고    scopus 로고
    • SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
    • Yoshida-Moriguchi T, et al. (2013) SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341(6148):896-899.
    • (2013) Science , vol.341 , Issue.6148 , pp. 896-899
    • Yoshida-Moriguchi, T.1
  • 6
    • 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
  • 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
  • 8
    • 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 , pp. e1002246
    • Eames, B.F.1
  • 9
    • 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
  • 10
    • 0033975514 scopus 로고    scopus 로고
    • Synthesis and sorting of proteoglycans
    • Prydz K, Dalen KT (2000) Synthesis and sorting of proteoglycans. J Cell Sci 113(Pt 2): 193-205.
    • (2000) J Cell Sci , vol.113 , Issue.2 , pp. 193-205
    • Prydz, K.1    Dalen, K.T.2
  • 12
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: Glycans as novel therapeutic targets
    • Fuster MM, Esko JD (2005) The sweet and sour of cancer: Glycans as novel therapeutic targets. Nat Rev Cancer 5(7):526-542.
    • (2005) Nat Rev Cancer , vol.5 , Issue.7 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 13
    • 17344369553 scopus 로고    scopus 로고
    • Mutations in the EXT1 and EXT2 genes in hereditary multiple exostoses
    • Wuyts W, et al. (1998) Mutations in the EXT1 and EXT2 genes in hereditary multiple exostoses. Am J Hum Genet 62(2):346-354.
    • (1998) Am J Hum Genet , vol.62 , Issue.2 , pp. 346-354
    • Wuyts, W.1
  • 14
    • 4143144349 scopus 로고    scopus 로고
    • Identification and molecular characterization of alpha-Liduronidase mutations present in mucopolysaccharidosis type I patients undergoing enzyme replacement therapy
    • Yogalingam G, et al. (2004) Identification and molecular characterization of alpha-Liduronidase mutations present in mucopolysaccharidosis type I patients undergoing enzyme replacement therapy. Hum Mutat 24(3):199-207.
    • (2004) Hum Mutat , vol.24 , Issue.3 , pp. 199-207
    • Yogalingam, G.1
  • 15
    • 80051542339 scopus 로고    scopus 로고
    • Faulty initiation of proteoglycan synthesis causes cardiac and joint defects
    • Baasanjav S, et al. (2011) Faulty initiation of proteoglycan synthesis causes cardiac and joint defects. Am J Hum Genet 89(1):15-27.
    • (2011) Am J Hum Genet , vol.89 , Issue.1 , pp. 15-27
    • Baasanjav, S.1
  • 16
    • 84878868522 scopus 로고    scopus 로고
    • Mutations in B3GALT6, which encodes a glycosaminoglycan linker region enzyme, cause a spectrum of skeletal and connective tissue disorders
    • Nakajima M, et al. (2013) Mutations in B3GALT6, which encodes a glycosaminoglycan linker region enzyme, cause a spectrum of skeletal and connective tissue disorders. Am J Hum Genet 92(6):927-934.
    • (2013) Am J Hum Genet , vol.92 , Issue.6 , pp. 927-934
    • Nakajima, M.1
  • 17
    • 84895923641 scopus 로고    scopus 로고
    • XYLT1 mutations in Desbuquois dysplasia type 2
    • Bui C, et al. (2014) XYLT1 mutations in Desbuquois dysplasia type 2. Am J Hum Genet 94(3):405-414.
    • (2014) Am J Hum Genet , vol.94 , Issue.3 , pp. 405-414
    • Bui, C.1
  • 20
    • 0030928652 scopus 로고    scopus 로고
    • Biosynthesis of the proteoglycan decorin-transient 2-phosphorylation of xylose during formation of the trisaccharide linkage region
    • Moses J, Oldberg A, Cheng F, Fransson LA (1997) Biosynthesis of the proteoglycan decorin-transient 2-phosphorylation of xylose during formation of the trisaccharide linkage region. Eur J Biochem 248(2):521-526.
    • (1997) Eur J Biochem , vol.248 , Issue.2 , pp. 521-526
    • Moses, J.1    Oldberg, A.2    Cheng, F.3    Fransson, L.A.4
  • 21
    • 73949158120 scopus 로고    scopus 로고
    • Decorin is processed by three isoforms of bone morphogenetic protein-1 (BMP1)
    • von Marschall Z, Fisher LW (2010) Decorin is processed by three isoforms of bone morphogenetic protein-1 (BMP1). Biochem Biophys Res Commun 391(3):1374-1378.
    • (2010) Biochem Biophys Res Commun , vol.391 , Issue.3 , pp. 1374-1378
    • Von Marschall, Z.1    Fisher, L.W.2
  • 22
    • 0035235423 scopus 로고    scopus 로고
    • Detection of proteoglycan core proteins with glycosaminoglycan lyases and antibodies
    • Couchman JR, Tapanadechopone P (2001) Detection of proteoglycan core proteins with glycosaminoglycan lyases and antibodies. Methods Mol Biol 171:329-333.
    • (2001) Methods Mol Biol , vol.171 , pp. 329-333
    • Couchman, J.R.1    Tapanadechopone, P.2
  • 23
    • 0024270443 scopus 로고
    • A new trisaccharide sugar chain linked to a serine residue in bovine blood coagulation factors VII and IX
    • Hase S, et al. (1988) A new trisaccharide sugar chain linked to a serine residue in bovine blood coagulation factors VII and IX. J Biochem 104(6):867-868.
    • (1988) J Biochem , vol.104 , Issue.6 , pp. 867-868
    • Hase, S.1
  • 24
    • 0034737738 scopus 로고    scopus 로고
    • Mammalian Notch1 is modified with two unusual forms of O-linked glycosylation found on epidermal growth factor-like modules
    • Moloney DJ, et al. (2000) Mammalian Notch1 is modified with two unusual forms of O-linked glycosylation found on epidermal growth factor-like modules. J Biol Chem 275(13):9604-9611.
    • (2000) J Biol Chem , vol.275 , Issue.13 , pp. 9604-9611
    • Moloney, D.J.1
  • 25
    • 77949896358 scopus 로고    scopus 로고
    • Mammalian Notch is modified by D-Xyl-alpha1-3-D-Xyl-alpha1-3-D-Glc-beta1-O-Ser: Implementation of a method to study O-glucosylation
    • Whitworth GE, Zandberg WF, Clark T, Vocadlo DJ (2010) Mammalian Notch is modified by D-Xyl-alpha1-3-D-Xyl-alpha1-3-D-Glc-beta1-O-Ser: Implementation of a method to study O-glucosylation. Glycobiology 20(3):287-299.
    • (2010) Glycobiology , vol.20 , Issue.3 , pp. 287-299
    • Whitworth, G.E.1    Zandberg, W.F.2    Clark, T.3    Vocadlo, D.J.4
  • 27
    • 66149149459 scopus 로고    scopus 로고
    • Analysis of N- and O-linked glycans from glycoproteins using MALDI-TOF mass spectrometry
    • Morelle W, Faid V, Chirat F, Michalski JC (2009) Analysis of N- and O-linked glycans from glycoproteins using MALDI-TOF mass spectrometry. Methods Mol Biol 534:5-21.
    • (2009) Methods Mol Biol , vol.534 , pp. 5-21
    • Morelle, W.1    Faid, V.2    Chirat, F.3    Michalski, J.C.4
  • 28
    • 0025677742 scopus 로고
    • Linkage analysis using Lindberg method
    • Hellerqvist CG (1990) Linkage analysis using Lindberg method. Methods Enzymol 193: 554-573.
    • (1990) Methods Enzymol , vol.193 , pp. 554-573
    • Hellerqvist, C.G.1
  • 29
    • 84862906051 scopus 로고    scopus 로고
    • Global metabolic inhibitors of sialyl- and fucosyltransferases remodel the glycome
    • Rillahan CD, et al. (2012) Global metabolic inhibitors of sialyl- and fucosyltransferases remodel the glycome. Nat Chem Biol 8(7):661-668.
    • (2012) Nat Chem Biol , vol.8 , Issue.7 , pp. 661-668
    • Rillahan, C.D.1
  • 30
    • 0035930615 scopus 로고    scopus 로고
    • Biosynthesis of the linkage region of glycosaminoglycans: Cloning and activity of galactosyltransferase II, the sixth member of the beta 1,3-galactosyltransferase family (beta 3GalT6)
    • Bai X, et al. (2001) Biosynthesis of the linkage region of glycosaminoglycans: cloning and activity of galactosyltransferase II, the sixth member of the beta 1,3-galactosyltransferase family (beta 3GalT6). J Biol Chem 276(51):48189-48195.
    • (2001) J Biol Chem , vol.276 , Issue.51 , pp. 48189-48195
    • Bai, X.1
  • 31
    • 47749118405 scopus 로고    scopus 로고
    • 2-o-phosphorylation of xylose and 6-o-sulfation of galactose in the protein linkage region of glycosaminoglycans influence the glucuronyltransfer-ase-I activity involved in the linkage region synthesis
    • Tone Y, et al. (2008) 2-o-phosphorylation of xylose and 6-o-sulfation of galactose in the protein linkage region of glycosaminoglycans influence the glucuronyltransfer-ase-I activity involved in the linkage region synthesis. J Biol Chem 283(24):16801-16807.
    • (2008) J Biol Chem , vol.283 , Issue.24 , pp. 16801-16807
    • Tone, Y.1
  • 32
    • 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
  • 33
    • 0037200168 scopus 로고    scopus 로고
    • Determination of the glycosaminoglycan-protein linkage region oligosaccharide structures of proteoglycans from Drosophila melanogaster and Caenorhabditis elegans
    • Yamada S, et al. (2002) Determination of the glycosaminoglycan-protein linkage region oligosaccharide structures of proteoglycans from Drosophila melanogaster and Caenorhabditis elegans. J Biol Chem 277(35):31877-31886.
    • (2002) J Biol Chem , vol.277 , Issue.35 , pp. 31877-31886
    • Yamada, S.1
  • 34
    • 0035800741 scopus 로고    scopus 로고
    • Structural characterization of heparan sulfate and chondroitin sulfate of syndecan-1 purified from normal murine mammary gland epithelial cells. Common phosphorylation of xylose and differential sulfation of galactose in the protein linkage region tetrasaccharide sequence
    • Ueno M, Yamada S, Zako M, Bernfield M, Sugahara K (2001) Structural characterization of heparan sulfate and chondroitin sulfate of syndecan-1 purified from normal murine mammary gland epithelial cells. Common phosphorylation of xylose and differential sulfation of galactose in the protein linkage region tetrasaccharide sequence. J Biol Chem 276(31):29134-29140.
    • (2001) J Biol Chem , vol.276 , Issue.31 , pp. 29134-29140
    • Ueno, M.1    Yamada, S.2    Zako, M.3    Bernfield, M.4    Sugahara, K.5
  • 35
    • 84896798726 scopus 로고    scopus 로고
    • Identification of phosphatase that dephosphorylates xylose in the glycosaminoglycan-protein linkage region of proteoglycans
    • Koike T, Izumikawa T, Sato B, Kitagawa H (2014) Identification of phosphatase that dephosphorylates xylose in the glycosaminoglycan-protein linkage region of proteoglycans. J Biol Chem 289(10):6695-6708.
    • (2014) J Biol Chem , vol.289 , Issue.10 , pp. 6695-6708
    • Koike, T.1    Izumikawa, T.2    Sato, B.3    Kitagawa, H.4
  • 36
    • 0025098286 scopus 로고
    • A genetic defect in the biosynthesis of dermatan sulfate proteoglycan: Galactosyltransferase I deficiency in fibroblasts from a patient with a progeroid syndrome
    • Quentin E, Gladen A, Rodén L, Kresse H (1990) A genetic defect in the biosynthesis of dermatan sulfate proteoglycan: Galactosyltransferase I deficiency in fibroblasts from a patient with a progeroid syndrome. Proc Natl Acad Sci USA 87(4):1342-1346.
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.4 , pp. 1342-1346
    • Quentin, E.1    Gladen, A.2    Rodén, L.3    Kresse, H.4
  • 37
    • 84891885235 scopus 로고    scopus 로고
    • The missing "link": An autosomal recessive short stature syndrome caused by a hypofunctional XYLT1 mutation
    • Schreml J, et al. (2014) The missing "link": An autosomal recessive short stature syndrome caused by a hypofunctional XYLT1 mutation. Hum Genet 133(1):29-39.
    • (2014) Hum Genet , vol.133 , Issue.1 , pp. 29-39
    • Schreml, J.1
  • 38
    • 84878827787 scopus 로고    scopus 로고
    • Defective initiation of glycosaminoglycan synthesis due to B3GALT6 mutations causes a pleiotropic Ehlers-Danlos-syndrome-like connective tissue disorder
    • Malfait F, et al. (2013) Defective initiation of glycosaminoglycan synthesis due to B3GALT6 mutations causes a pleiotropic Ehlers-Danlos-syndrome-like connective tissue disorder. Am J Hum Genet 92(6):935-945.
    • (2013) Am J Hum Genet , vol.92 , Issue.6 , pp. 935-945
    • Malfait, F.1
  • 39
    • 64749109053 scopus 로고    scopus 로고
    • An efficient platform for screening expression and crystallization of glycoproteins produced in human cells
    • Lee JE, Fusco ML, Saphire EO (2009) An efficient platform for screening expression and crystallization of glycoproteins produced in human cells. Nat Protoc 4(4):592-604.
    • (2009) Nat Protoc , vol.4 , Issue.4 , pp. 592-604
    • Lee, J.E.1    Fusco, M.L.2    Saphire, E.O.3
  • 40
    • 0141763811 scopus 로고    scopus 로고
    • The role of decorin in collagen fibrillogenesis and skin homeostasis
    • Reed CC, Iozzo RV (2002) The role of decorin in collagen fibrillogenesis and skin homeostasis. Glycoconj J 19(4-5):249-255.
    • (2002) Glycoconj J , vol.19 , Issue.4-5 , pp. 249-255
    • Reed, C.C.1    Iozzo, R.V.2
  • 41
    • 16244380777 scopus 로고    scopus 로고
    • Syndecans: New kids on the signaling block
    • Tkachenko E, Rhodes JM, Simons M (2005) Syndecans: New kids on the signaling block. Circ Res 96(5):488-500.
    • (2005) Circ Res , vol.96 , Issue.5 , pp. 488-500
    • Tkachenko, E.1    Rhodes, J.M.2    Simons, M.3
  • 42
    • 84859986516 scopus 로고    scopus 로고
    • Crystal structure of N-glycosylated human glypican-1 core protein: Structure of two loops evolutionarily conserved in vertebrate glypican-1
    • Svensson G, Awad W, Håkansson M, Mani K, Logan DT (2012) Crystal structure of N-glycosylated human glypican-1 core protein: structure of two loops evolutionarily conserved in vertebrate glypican-1. J Biol Chem 287(17):14040-14051.
    • (2012) J Biol Chem , vol.287 , Issue.17 , pp. 14040-14051
    • Svensson, G.1    Awad, W.2    Håkansson, M.3    Mani, K.4    Logan, D.T.5
  • 43
    • 72149110399 scopus 로고    scopus 로고
    • Breaking the code of DNA binding specificity of TAL-type III effectors
    • Boch J, et al. (2009) Breaking the code of DNA binding specificity of TAL-type III effectors. Science 326(5959):1509-1512.
    • (2009) Science , vol.326 , Issue.5959 , pp. 1509-1512
    • Boch, J.1
  • 44
    • 79960064013 scopus 로고    scopus 로고
    • Efficient design and assembly of custom TALEN and other TAL effector-based constructs for DNA targeting
    • Cermak T, et al. (2011) Efficient design and assembly of custom TALEN and other TAL effector-based constructs for DNA targeting. Nucleic Acids Res 39(12):e82.
    • (2011) Nucleic Acids Res , vol.39 , Issue.12 , pp. e82
    • Cermak, T.1
  • 45
    • 1842579613 scopus 로고    scopus 로고
    • Mutation detection using Surveyor nuclease
    • Qiu P, et al. (2004) Mutation detection using Surveyor nuclease. Biotechniques 36(4): 702-707.
    • (2004) Biotechniques , vol.36 , Issue.4 , pp. 702-707
    • Qiu, P.1
  • 46
    • 84901918918 scopus 로고    scopus 로고
    • Sialylation of outer membrane porin protein D: A mechanistic basis of antibiotic uptake in Pseudomonas aeruginosa
    • Khatua B, Van Vleet J, Choudhury BP, Chaudhry R, Mandal C (2014) Sialylation of outer membrane porin protein D: A mechanistic basis of antibiotic uptake in Pseudomonas aeruginosa. Mol Cell Proteomics 13(6):1412-1428.
    • (2014) Mol Cell Proteomics , vol.13 , Issue.6 , pp. 1412-1428
    • Khatua, B.1    Van Vleet, J.2    Choudhury, B.P.3    Chaudhry, R.4    Mandal, C.5
  • 47
    • 34447326804 scopus 로고
    • A simple and rapid method for the permethylation of carbohydrates
    • Ciucanu I, Kerek F (1984) A simple and rapid method for the permethylation of carbohydrates. Carbohydr Res 131(2):209-217.
    • (1984) Carbohydr Res , vol.131 , Issue.2 , pp. 209-217
    • Ciucanu, I.1    Kerek, F.2
  • 48
    • 84869475601 scopus 로고    scopus 로고
    • The GlycanBuilder and GlycoWorkbench glycoinformatics tools: Updates and new developments
    • Damerell D, et al. (2012) The GlycanBuilder and GlycoWorkbench glycoinformatics tools: Updates and new developments. Biol Chem 393(11):1357-1362.
    • (2012) Biol Chem , vol.393 , Issue.11 , pp. 1357-1362
    • Damerell, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.