메뉴 건너뛰기




Volumn 5, Issue APRIL2016, 2016, Pages

The functional O-mannose glycan on α-dystroglycan contains a phospho-ribitol primed for matriglycan addition

(16)  Praissman, Jeremy L a   Willer, Tobias b,c   Osman Sheikh, M a   Toi, Ants d   Chitayat, David d,e,f   Lin, Yung Yao g,h   Lee, Hane i,j   Stalnaker, Stephanie H a   Wang, Shuo a   Prabhakar, Pradeep Kumar a   Nelson, Stanley F i,j   Stemple, Derek L h   Moore, Steven A b   Moremen, Kelley W a   Campbell, Kevin P b,c   Wells, Lance a  


Author keywords

[No Author keywords available]

Indexed keywords

ALPHA DYSTROGLYCAN; GLYCAN DERIVATIVE; PEPTIDES AND PROTEINS; PROTEIN P53; RIBITOL; TMEM5 PROTEIN; UNCLASSIFIED DRUG; DAG1 PROTEIN, HUMAN; DYSTROGLYCAN; ISPD PROTEIN, HUMAN; MANNOSE; MEMBRANE PROTEIN; NUCLEOTIDYLTRANSFERASE; POLYSACCHARIDE; PROTEIN BINDING; TMEM5 PROTEIN, HUMAN;

EID: 84979503456     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.14473     Document Type: Article
Times cited : (87)

References (60)
  • 1
    • 84878799611 scopus 로고    scopus 로고
    • Predicting functional effect of human missense mutations using polyphen-2
    • Adzhubei I, Jordan DM, Sunyaev SR. 2013. Predicting functional effect of human missense mutations using polyphen-2. Curr Protoc Hum Genet Chapter 7, Unit 7 20: 7.20.1-7.20.7. doi: 10.1002/0471142905.hg0720s76.
    • (2013) Curr Protoc Hum Genet Chapter 7, Unit 7 , vol.20 , pp. 7.20.1-7.20.7
    • Adzhubei, I.1    Jordan, D.M.2    Sunyaev, S.R.3
  • 2
    • 77049285781 scopus 로고
    • The isolation of cytidine diphosphate glycerol, cytidine diphosphate ribitol and mannitol 1-phosphate from lactobacillus arabinosus
    • Baddiley J, Buchanan JG, Carss B, Mathias A.P, Sanderson AR. 1956. The isolation of cytidine diphosphate glycerol, cytidine diphosphate ribitol and mannitol 1-phosphate from lactobacillus arabinosus. The Biochemical Journal 64: 599-603. doi: 10.1042/bj0640599.
    • (1956) The Biochemical Journal , vol.64 , pp. 599-603
    • Baddiley, J.1    Buchanan, J.G.2    Carss, B.3    Mathias, A.P.4    Sanderson, A.R.5
  • 3
    • 84861883015 scopus 로고    scopus 로고
    • NMR characterization of immunoglobulin G fc glycan motion on enzymatic sialylation
    • Barb AW, Meng L, Gao Z, Johnson RW, Moremen KW, Prestegard JH. 2012. NMR characterization of immunoglobulin G fc glycan motion on enzymatic sialylation. Biochemistry 51: 4618-4626. doi: 10.1021/bi300319q.
    • (2012) Biochemistry , vol.51 , pp. 4618-4626
    • Barb, A.W.1    Meng, L.2    Gao, Z.3    Johnson, R.W.4    Moremen, K.W.5    Prestegard, J.H.6
  • 5
    • 60849110560 scopus 로고    scopus 로고
    • Synthesis of cdp-activated ribitol for teichoic acid precursors in streptococcus pneumoniae
    • Baur S, Marles-Wright J, Buckenmaier S, Lewis RJ, Vollmer W. 2009. Synthesis of cdp-activated ribitol for teichoic acid precursors in streptococcus pneumoniae. Journal of Bacteriology 191: 1200-1210. doi: 10.1128/JB.01120-08.
    • (2009) Journal of Bacteriology , vol.191 , pp. 1200-1210
    • Baur, S.1    Marles-Wright, J.2    Buckenmaier, S.3    Lewis, R.J.4    Vollmer, W.5
  • 6
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett D, Kovaleva E, Schatz PJ. 1999. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Science 8: 921-929. doi: 10.1110/ps.8.4.921.
    • (1999) Protein Science , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 8
    • 82755181721 scopus 로고    scopus 로고
    • Cell-matrix interactions in muscle disease
    • Carmignac V, Durbeej M. 2012. Cell-matrix interactions in muscle disease. The Journal of Pathology 226: 200-218. doi: 10.1002/path.3020.
    • (2012) The Journal of Pathology , vol.226 , pp. 200-218
    • Carmignac, V.1    Durbeej, M.2
  • 9
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin
    • Chiba A, Matsumura K, Yamada H, Inazu T, Shimizu T, Kusunoki S, Kanazawa I, Kobata A, Endo T. 1997. Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin. The Journal of Biological Chemistry 272: 2156-2162.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yamada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6    Kanazawa, I.7    Kobata, A.8    Endo, T.9
  • 14
    • 84925946372 scopus 로고    scopus 로고
    • DAG1 mutations associated with asymptomatic hyperckemia and hypoglycosylation of α-dystroglycan
    • Dong M, Noguchi S, Endo Y, Hayashi YK, Yoshida S, Nonaka I, Nishino I. 2015. DAG1 mutations associated with asymptomatic hyperckemia and hypoglycosylation of α-dystroglycan. Neurology 84: 273-279. doi: 10.1212/WNL.0000000000001162.
    • (2015) Neurology , vol.84 , pp. 273-279
    • Dong, M.1    Noguchi, S.2    Endo, Y.3    Hayashi, Y.K.4    Yoshida, S.5    Nonaka, I.6    Nishino, I.7
  • 16
    • 36849039236 scopus 로고    scopus 로고
    • O-mannosylation in mammalian cells
    • Endo T, Manya H. 2006. O-mannosylation in mammalian cells. Methods in Molecular Biology 347: 43-56. doi: 10.1385/1-59745-167-3: 43.
    • (2006) Methods in Molecular Biology , vol.347 , pp. 43-56
    • Endo, T.1    Manya, H.2
  • 17
    • 84941114402 scopus 로고    scopus 로고
    • Glycobiology of α-dystroglycan and muscular dystrophy
    • Endo T. 2015. Glycobiology of α-dystroglycan and muscular dystrophy. Journal of Biochemistry 157: 1-12. doi: 10.1093/jb/mvu066.
    • (2015) Journal of Biochemistry , vol.157 , pp. 1-12
    • Endo, T.1
  • 18
    • 0025272250 scopus 로고
    • Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle
    • Ervasti JM, Ohlendieck K, Kahl SD, Gaver MG, Campbell KP. 1990. Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle. Nature 345: 315-319. doi: 10.1038/345315a0.
    • (1990) Nature , vol.345 , pp. 315-319
    • Ervasti, J.M.1    Ohlendieck, K.2    Kahl, S.D.3    Gaver, M.G.4    Campbell, K.P.5
  • 19
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti JM, Campbell KP. 1991. Membrane organization of the dystrophin-glycoprotein complex. Cell 66: 1121-1131. doi: 10.1016/0092-8674(91)90035-W.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 24
    • 0033976679 scopus 로고    scopus 로고
    • Biosynthesis of dystroglycan: Processing of a precursor propeptide
    • Holt KH, Crosbie RH, Venzke DP, Campbell KP. 2000. Biosynthesis of dystroglycan: Processing of a precursor propeptide. FEBS Letters 468: 79-83. doi: 10.1016/S0014-5793(00)01195-9.
    • (2000) FEBS Letters , vol.468 , pp. 79-83
    • Holt, K.H.1    Crosbie, R.H.2    Venzke, D.P.3    Campbell, K.P.4
  • 27
    • 84884274063 scopus 로고    scopus 로고
    • In-gel b-elimination and aqueous-organic partition for improved O- and sulfoglycomics
    • Kumagai T, Katoh T, Nix DB, Tiemeyer M, Aoki K. 2013. In-gel b-elimination and aqueous-organic partition for improved O- and sulfoglycomics. Analytical Chemistry 85: 8692-8699. doi: 10.1021/ac4015935.
    • (2013) Analytical Chemistry , vol.85 , pp. 8692-8699
    • Kumagai, T.1    Katoh, T.2    Nix, D.B.3    Tiemeyer, M.4    Aoki, K.5
  • 28
    • 56549084586 scopus 로고    scopus 로고
    • Phenotypic and genetic analysis of a large family with migraine-associated vertigo
    • Lee H, Jen JC, Cha YH, Nelson SF, Baloh RW. 2008. Phenotypic and genetic analysis of a large family with migraine-associated vertigo. Headache 48: 1460-1467. doi: 10.1111/j.1526-4610.2007.01002.x.
    • (2008) Headache , vol.48 , pp. 1460-1467
    • Lee, H.1    Jen, J.C.2    Cha, Y.H.3    Nelson, S.F.4    Baloh, R.W.5
  • 29
    • 74549201511 scopus 로고    scopus 로고
    • Improving the efficiency of genomic loci capture using oligonucleotide arrays for high throughput resequencing
    • Lee H, O’Connor BD, Merriman B, Funari VA, Homer N, Chen Z, Cohn DH, Nelson SF. 2009. Improving the efficiency of genomic loci capture using oligonucleotide arrays for high throughput resequencing. BMCGenomics 10: 646: 646. doi: 10.1186/1471-2164-10-646.
    • (2009) BMCGenomics , vol.10 , Issue.646 , pp. 646
    • Lee, H.1    O’Connor, B.D.2    Merriman, B.3    Funari, V.A.4    Homer, N.5    Chen, Z.6    Cohn, D.H.7    Nelson, S.F.8
  • 30
    • 84865229984 scopus 로고    scopus 로고
    • Developmental expression of the neuron-specific n-acetylglucosaminyltransferase vb (GnT-Vb/IX) and identification of its in vivo glycan products in comparison with those of its paralog, GnT-V
    • Lee JK, Matthews RT, Lim JM, Swanier K, Wells L, Pierce JM. 2012. Developmental expression of the neuron-specific n-acetylglucosaminyltransferase vb (GnT-Vb/IX) and identification of its in vivo glycan products in comparison with those of its paralog, GnT-V. The Journal of Biological Chemistry 287: 28526-28536. doi: 10.1074/jbc.M112.367565.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 28526-28536
    • Lee, J.K.1    Matthews, R.T.2    Lim, J.M.3    Swanier, K.4    Wells, L.5    Pierce, J.M.6
  • 36
    • 80052472115 scopus 로고    scopus 로고
    • Muscular dystrophies due to glycosylation defects: Diagnosis and therapeutic strategies
    • Muntoni F, Torelli S, Wells DJ, Brown SC. 2011. Muscular dystrophies due to glycosylation defects: Diagnosis and therapeutic strategies. Current Opinion in Neurology 24: 437-442. doi: 10.1097/WCO.0b013e32834a95e3.
    • (2011) Current Opinion in Neurology , vol.24 , pp. 437-442
    • Muntoni, F.1    Torelli, S.2    Wells, D.J.3    Brown, S.C.4
  • 37
    • 0036637659 scopus 로고    scopus 로고
    • Removal of dystroglycan causes severe muscular dystrophy in zebrafish embryos
    • Parsons MJ, Campos I, Hirst EM, Stemple DL. 2002. Removal of dystroglycan causes severe muscular dystrophy in zebrafish embryos. Development 129: 3505-3512.
    • (2002) Development , vol.129 , pp. 3505-3512
    • Parsons, M.J.1    Campos, I.2    Hirst, E.M.3    Stemple, D.L.4
  • 38
    • 79960221714 scopus 로고    scopus 로고
    • Oxidative stress, inflammation and carcinogenesis are controlled through the pentose phosphate pathway by transaldolase
    • Perl A, Hanczko R, Telarico T, Oaks Z, Landas S. 2011. Oxidative stress, inflammation and carcinogenesis are controlled through the pentose phosphate pathway by transaldolase. Trends in Molecular Medicine 17: 395-403. doi: 10.1016/j.molmed.2011.01.014.
    • (2011) Trends in Molecular Medicine , vol.17 , pp. 395-403
    • Perl, A.1    Hanczko, R.2    Telarico, T.3    Oaks, Z.4    Landas, S.5
  • 39
    • 84901036287 scopus 로고    scopus 로고
    • Mammalian o-mannosylation pathway: Glycan structures, enzymes, and protein substrates
    • Praissman JL, Wells L. 2014. Mammalian o-mannosylation pathway: Glycan structures, enzymes, and protein substrates. Biochemistry 53: 3066-3078. doi: 10.1021/bi500153y.
    • (2014) Biochemistry , vol.53 , pp. 3066-3078
    • Praissman, J.L.1    Wells, L.2
  • 40
    • 85016162643 scopus 로고    scopus 로고
    • B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycan
    • Praissman JL, Live DH, Wang S, Ramiah A, Chinoy ZS, Boons GJ, Moremen KW, Wells L. 2014. B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycan. eLife 3:e03943. doi: 10.7554/eLife.03943.
    • (2014) eLife , vol.3 , pp. e03943
    • Praissman, J.L.1    Live, D.H.2    Wang, S.3    Ramiah, A.4    Chinoy, Z.S.5    Boons, G.J.6    Moremen, K.W.7    Wells, L.8
  • 42
  • 47
    • 84864430562 scopus 로고    scopus 로고
    • SIFT web server: Predicting effects of amino acid substitutions on proteins
    • Sim NL, Kumar P, Hu J, Henikoff S, Schneider G, Ng PC. 2012. SIFT web server: Predicting effects of amino acid substitutions on proteins. Nucleic Acids Research 40:W452-457. doi: 10.1093/nar/gks539.
    • (2012) Nucleic Acids Research , vol.40 , pp. W452-W457
    • Sim, N.L.1    Kumar, P.2    Hu, J.3    Henikoff, S.4    Schneider, G.5    Ng, P.C.6
  • 49
    • 80053572638 scopus 로고    scopus 로고
    • Mammalian o-mannosylation: Unsolved questions of structure/function
    • Stalnaker SH, Stuart R, Wells L. 2011. Mammalian o-mannosylation: Unsolved questions of structure/function. Current Opinion in Structural Biology 21: 603-609. doi: 10.1016/j.sbi.2011.09.001.
    • (2011) Current Opinion in Structural Biology , vol.21 , pp. 603-609
    • Stalnaker, S.H.1    Stuart, R.2    Wells, L.3
  • 53
    • 84874883376 scopus 로고    scopus 로고
    • The o-mannosylation pathway: Glycosyltransferases and proteins implicated in congenital muscular dystrophy
    • Wells L. 2013. The o-mannosylation pathway: Glycosyltransferases and proteins implicated in congenital muscular dystrophy. The Journal of Biological Chemistry 288: 6930-6935. doi: 10.1074/jbc.R112.438978.
    • (2013) The Journal of Biological Chemistry , vol.288 , pp. 6930-6935
    • Wells, L.1
  • 56
    • 0025242185 scopus 로고
    • Glycoprotein complex anchoring dystrophin to sarcolemma
    • Yoshida M, Ozawa E. 1990. Glycoprotein complex anchoring dystrophin to sarcolemma. Journal of Biochemistry 108: 748-752.
    • (1990) Journal of Biochemistry , vol.108 , pp. 748-752
    • Yoshida, M.1    Ozawa, E.2
  • 60
    • 84936755861 scopus 로고    scopus 로고
    • Matriglycan: A novel polysaccharide that links dystroglycan to the basement membrane
    • Yoshida-Moriguchi T, Campbell KP. 2015. Matriglycan: A novel polysaccharide that links dystroglycan to the basement membrane. Glycobiology 25: 702-713. doi: 10.1093/glycob/cwv021.
    • (2015) Glycobiology , vol.25 , pp. 702-713
    • Yoshida-Moriguchi, T.1    Campbell, K.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.