메뉴 건너뛰기




Volumn 25, Issue 8, 2016, Pages 1489-1500

Glycosylation abnormalities in Gdt1p/TMEM165 deficient cells result from a defect in Golgi manganese homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; MANGANESE; MEMBRANE PROTEIN; TMEM165 PROTEIN; UNCLASSIFIED DRUG; FUNGAL PROTEIN; GOLIM4 PROTEIN, HUMAN; TMEM165 PROTEIN, HUMAN; VESICULAR TRANSPORT PROTEIN;

EID: 84963725172     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddw026     Document Type: Article
Times cited : (90)

References (35)
  • 1
    • 84904111497 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: new defects and still counting
    • Scott, K., Gadomski, T., Kozicz, T. and Morava, E. (2014) Congenital disorders of glycosylation: new defects and still counting. J. Inherit. Metab. Dis., 37, 609-617.
    • (2014) J. Inherit. Metab. Dis. , vol.37 , pp. 609-617
    • Scott, K.1    Gadomski, T.2    Kozicz, T.3    Morava, E.4
  • 2
    • 84874901762 scopus 로고    scopus 로고
    • Understanding human glycosylation disorders: biochemistry leads the charge
    • Freeze, H.H. (2013) Understanding human glycosylation disorders: biochemistry leads the charge. J. Biol. Chem., 288, 6936-6945.
    • (2013) J. Biol. Chem. , vol.288 , pp. 6936-6945
    • Freeze, H.H.1
  • 4
    • 84876835227 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation
    • Jaeken, J. (2013) Congenital disorders of glycosylation. Handb. Clin. Neurol., 113, 1737-1743.
    • (2013) Handb. Clin. Neurol. , vol.113 , pp. 1737-1743
    • Jaeken, J.1
  • 5
    • 34250903593 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: CDG-I, CDG-II, and beyond
    • Freeze, H.H. (2007) Congenital disorders of glycosylation: CDG-I, CDG-II, and beyond. Curr. Mol. Med., 7, 389-396.
    • (2007) Curr. Mol. Med. , vol.7 , pp. 389-396
    • Freeze, H.H.1
  • 6
    • 35548972537 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: a rapidly expanding disease family
    • Jaeken, J. and Matthijs, G. (2007) Congenital disorders of glycosylation: a rapidly expanding disease family. Annu. Rev. Genomics Hum. Genet., 8, 261-278.
    • (2007) Annu. Rev. Genomics Hum. Genet. , vol.8 , pp. 261-278
    • Jaeken, J.1    Matthijs, G.2
  • 7
    • 84893734160 scopus 로고    scopus 로고
    • Solving glycosylation disorders: fundamental approaches reveal complicated pathways
    • Freeze, H.H., Chong, J.X., Bamshad, M.J. and Ng, B.G. (2014) Solving glycosylation disorders: fundamental approaches reveal complicated pathways. Am. J. Hum. Genet., 94, 161-175.
    • (2014) Am. J. Hum. Genet. , vol.94 , pp. 161-175
    • Freeze, H.H.1    Chong, J.X.2    Bamshad, M.J.3    Ng, B.G.4
  • 9
    • 0027930443 scopus 로고
    • Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II
    • Jaeken, J., Schachter, H., Carchon, H., De Cock, P., Coddeville, B. and Spik, G. (1994) Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II. Arch. Dis. Child., 71, 123-127.
    • (1994) Arch. Dis. Child. , vol.71 , pp. 123-127
    • Jaeken, J.1    Schachter, H.2    Carchon, H.3    De Cock, P.4    Coddeville, B.5    Spik, G.6
  • 10
    • 15944399952 scopus 로고    scopus 로고
    • Genetic complementation reveals a novel human congenital disorder of glycosylation of type II, due to inactivation of the Golgi CMP-sialic acid transporter
    • Martinez-Duncker, I., Dupré, T., Piller, V., Piller, F., Candelier, J.-J., Trichet, C., Tchernia, G., Oriol, R. and Mollicone, R. (2005) Genetic complementation reveals a novel human congenital disorder of glycosylation of type II, due to inactivation of the Golgi CMP-sialic acid transporter. Blood, 105, 2671-2676.
    • (2005) Blood , vol.105 , pp. 2671-2676
    • Martinez-Duncker, I.1    Dupré, T.2    Piller, V.3    Piller, F.4    Candelier, J.-J.5    Trichet, C.6    Tchernia, G.7    Oriol, R.8    Mollicone, R.9
  • 18
    • 84952308445 scopus 로고    scopus 로고
    • High-resolution mass spectrometry glycoprofiling of intact transferrin for diagnosis and subtype identification in the congenital disorders of glycosylation
    • Van Scherpenzeel, M., Steenbergen, G., Morava, E.,Wevers, R. A. and Lefeber, D.J. High-resolution mass spectrometry glycoprofiling of intact transferrin for diagnosis and subtype identification in the congenital disorders of glycosylation. Transl. Res., doi: 10.1016/j.trsl.2015.07.005.
    • Transl. Res.
    • Van Scherpenzeel, M.1    Steenbergen, G.2    Morava, E.3    Wevers, R.A.4    Lefeber, D.J.5
  • 22
    • 0031664331 scopus 로고    scopus 로고
    • The medial-Golgi ion pump Pmr1 supplies the yeast secretory pathway with Ca2+ and Mn2+ required for glycosylation, sorting, and endoplasmic reticulum-associated protein degradation
    • Dürr, G., Strayle, J., Plemper, R., Elbs, S., Klee, S.K., Catty, P., Wolf, D.H. and Rudolph, H.K. (1998) The medial-Golgi ion pump Pmr1 supplies the yeast secretory pathway with Ca2+ and Mn2+ required for glycosylation, sorting, and endoplasmic reticulum-associated protein degradation. Mol. Biol. Cell, 9, 1149-1162.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1149-1162
    • Dürr, G.1    Strayle, J.2    Plemper, R.3    Elbs, S.4    Klee, S.K.5    Catty, P.6    Wolf, D.H.7    Rudolph, H.K.8
  • 23
    • 0027097849 scopus 로고
    • (2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution
    • (2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell, 3, 633-654.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 633-654
    • Antebi, A.1    Fink, G.R.2
  • 24
    • 84876434668 scopus 로고    scopus 로고
    • Regulation of cation balance in Saccharomyces cerevisiae
    • Cyert, M.S. and Philpott, C.C. (2013) Regulation of cation balance in Saccharomyces cerevisiae. Genetics, 193, 677-713.
    • (2013) Genetics , vol.193 , pp. 677-713
    • Cyert, M.S.1    Philpott, C.C.2
  • 25
    • 33644883005 scopus 로고    scopus 로고
    • A global view of pleiotropy and phenotypically derived gene function in yeast
    • 2005.0001
    • Dudley, A.M., Janse, D.M., Tanay, A., Shamir, R. and Church, G. M. (2005) A global view of pleiotropy and phenotypically derived gene function in yeast. Mol. Syst. Biol., 1, 2005.0001.
    • (2005) Mol. Syst. Biol. , vol.1
    • Dudley, A.M.1    Janse, D.M.2    Tanay, A.3    Shamir, R.4    Church, G.M.5
  • 26
    • 32944479485 scopus 로고    scopus 로고
    • MNN5 encodes an iron-regulated alpha-1,2-mannosyltransferase important for protein glycosylation, cell wall integrity, morphogenesis, and virulence in Candida albicans
    • Bai, C., Xu, X.-L., Chan, F.-Y., Lee, R.T.H. and Wang, Y. (2006) MNN5 encodes an iron-regulated alpha-1,2-mannosyltransferase important for protein glycosylation, cell wall integrity, morphogenesis, and virulence in Candida albicans. Eukaryot. Cell, 5, 238-247.
    • (2006) Eukaryot. Cell , vol.5 , pp. 238-247
    • Bai, C.1    Xu, X.-L.2    Chan, F.-Y.3    Lee, R.T.H.4    Wang, Y.5
  • 27
    • 84875497828 scopus 로고    scopus 로고
    • Golgi phosphoprotein 4 (GPP130) is a sensitive and selective cellular target of manganese exposure
    • Masuda, M., Braun-sommargren, M., Crooks, D. and Smith, D. R. (2013) Golgi phosphoprotein 4 (GPP130) is a sensitive and selective cellular target of manganese exposure. Synapse NY, 67, 205-215.
    • (2013) Synapse NY , vol.67 , pp. 205-215
    • Masuda, M.1    Braun-sommargren, M.2    Crooks, D.3    Smith, D.R.4
  • 28
    • 77950687021 scopus 로고    scopus 로고
    • Manganese-induced trafficking and turnover of the cis- Golgi glycoprotein GPP130
    • Mukhopadhyay, S., Bachert, C., Smith, D.R. and Linstedt, A.D. (2010) Manganese-induced trafficking and turnover of the cis- Golgi glycoprotein GPP130. Mol. Biol. Cell, 21, 1282-1292.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1282-1292
    • Mukhopadhyay, S.1    Bachert, C.2    Smith, D.R.3    Linstedt, A.D.4
  • 29
    • 0032493440 scopus 로고    scopus 로고
    • Activity of the yeast MNN1 alpha- 1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases
    • Ca,W. and Munro, S. (1998) Activity of the yeast MNN1 alpha- 1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases. Proc. Natl. Acad. Sci. USA, 95, 7945-7950.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7945-7950
    • Ca, W.1    Munro, S.2
  • 30
    • 0032500541 scopus 로고    scopus 로고
    • Identification of the MNN2 and MNN5 mannosyltransferases required for forming and extending the mannose branches of the outer chain mannans of Saccharomyces cerevisiae
    • Rayner, J.C. and Munro, S. (1998) Identification of the MNN2 and MNN5 mannosyltransferases required for forming and extending the mannose branches of the outer chain mannans of Saccharomyces cerevisiae. J. Biol. Chem., 273, 26836-26843.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26836-26843
    • Rayner, J.C.1    Munro, S.2
  • 33
    • 0025313449 scopus 로고
    • Isolation, characterization, and properties of Saccharomyces cerevisiae mnn mutants with nonconditional protein glycosylation defects
    • Academic Press, USA
    • Ballou, C.E.(1990) Isolation, characterization, and properties of Saccharomyces cerevisiae mnn mutants with nonconditional protein glycosylation defects. Gene Expression Technology (Methods Enzymology). Academic Press, USA, Vol. 185, pp. 440-470.
    • (1990) Gene Expression Technology (Methods Enzymology) , vol.185 , pp. 440-470
    • Ballou, C.E.1
  • 34
    • 34447097453 scopus 로고    scopus 로고
    • Analysis of protein glycosylation by mass spectrometry
    • Morelle,W. and Michalski, J.-C. (2007) Analysis of protein glycosylation by mass spectrometry. Nat. Protoc., 2, 1585-1602.
    • (2007) Nat. Protoc. , vol.2 , pp. 1585-1602
    • Morelle, W.1    Michalski, J.-C.2
  • 35
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C.A., Rasband, W.S. and Eliceiri, K.W. (2012) NIH Image to ImageJ: 25 years of image analysis. Nat. Methods, 9, 671-675.
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.