메뉴 건너뛰기




Volumn 6, Issue 11, 2011, Pages

The two Caenorhabditis elegans UDP-glucose:Glycoprotein glucosyltransferase homologues have distinct biological functions

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; GREEN FLUORESCENT PROTEIN; TUNICAMYCIN; UDP GLUCOSE GLYCOPROTEIN GLUCOSYLTRANSFERASE; UNCLASSIFIED DRUG; GLUCOSYLTRANSFERASE; ISOENZYME; MANNOSYLGLYCOPROTEIN 1,3 GLUCOSYLTRANSFERASE; MANNOSYLGLYCOPROTEIN 1,3-GLUCOSYLTRANSFERASE; PRIMER DNA;

EID: 80355143396     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0027025     Document Type: Article
Times cited : (25)

References (34)
  • 1
    • 0026799435 scopus 로고
    • Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase
    • Trombetta SE, Parodi AJ, (1992) Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase. J Biol Chem 267: 9236-9240.
    • (1992) J Biol Chem , vol.267 , pp. 9236-9240
    • Trombetta, S.E.1    Parodi, A.J.2
  • 2
    • 0037743618 scopus 로고    scopus 로고
    • The UDP-glucose:glycoprotein glucosyltransferase is organized in at least two tightly bound domains from yeast to mammals
    • Guerin M, Parodi AJ, (2003) The UDP-glucose:glycoprotein glucosyltransferase is organized in at least two tightly bound domains from yeast to mammals. J Biol Chem 278: 20540-20546.
    • (2003) J Biol Chem , vol.278 , pp. 20540-20546
    • Guerin, M.1    Parodi, A.J.2
  • 3
    • 36249022072 scopus 로고    scopus 로고
    • How sugars convey information on protein conformation in the endoplasmic reticulum
    • Caramelo JJ, Parodi AJ, (2007) How sugars convey information on protein conformation in the endoplasmic reticulum. Semin Cell Dev Biol 18: 732-742.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 732-742
    • Caramelo, J.J.1    Parodi, A.J.2
  • 4
    • 0025339572 scopus 로고
    • The yeast KRE5 gene encodes a probable endoplasmic reticulum protein required for (1-6)-beta-D-glucan synthesis and normal cell growth
    • Meaden P, Hill K, Wagner J, Slipetz D, Sommer SS, et al. (1990) The yeast KRE5 gene encodes a probable endoplasmic reticulum protein required for (1-6)-beta-D-glucan synthesis and normal cell growth. Mol Cell Biol 10: 3013-3019.
    • (1990) Mol Cell Biol , vol.10 , pp. 3013-3019
    • Meaden, P.1    Hill, K.2    Wagner, J.3    Slipetz, D.4    Sommer, S.S.5
  • 5
    • 0030020169 scopus 로고    scopus 로고
    • A new stress protein: synthesis of Schizosaccharomyces pombe UDP-Glc:glycoprotein glucosyltransferase mRNA is induced by stress conditions but the enzyme is not essential for cell viability
    • Fernandez F, Jannatipour M, Hellman U, Rokeach LA, Parodi AJ, (1996) A new stress protein: synthesis of Schizosaccharomyces pombe UDP-Glc:glycoprotein glucosyltransferase mRNA is induced by stress conditions but the enzyme is not essential for cell viability. EMBO J 15: 705-713.
    • (1996) EMBO J , vol.15 , pp. 705-713
    • Fernandez, F.1    Jannatipour, M.2    Hellman, U.3    Rokeach, L.A.4    Parodi, A.J.5
  • 6
    • 0141521671 scopus 로고    scopus 로고
    • The interplay between folding-facilitating mechanisms in Trypanosoma cruzi endoplasmic reticulum
    • Conte I, Labriola C, Cazzulo JJ, Docampo R, Parodi AJ, (2003) The interplay between folding-facilitating mechanisms in Trypanosoma cruzi endoplasmic reticulum. Mol Biol Cell 14: 3529-3540.
    • (2003) Mol Biol Cell , vol.14 , pp. 3529-3540
    • Conte, I.1    Labriola, C.2    Cazzulo, J.J.3    Docampo, R.4    Parodi, A.J.5
  • 7
    • 0028987945 scopus 로고
    • Drosophila UDP-glucose:glycoprotein glucosyltransferase: sequence and characterization of an enzyme that distinguishes between denatured and native proteins
    • Parker CG, Fessler LI, Nelson RE, Fessler JH, (1995) Drosophila UDP-glucose:glycoprotein glucosyltransferase: sequence and characterization of an enzyme that distinguishes between denatured and native proteins. EMBO J 14: 1294-1303.
    • (1995) EMBO J , vol.14 , pp. 1294-1303
    • Parker, C.G.1    Fessler, L.I.2    Nelson, R.E.3    Fessler, J.H.4
  • 8
    • 0034010855 scopus 로고    scopus 로고
    • Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity
    • Arnold SM, Fessler LI, Fessler JH, Kaufman RJ, (2000) Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity. Biochemistry 39: 2149-2163.
    • (2000) Biochemistry , vol.39 , pp. 2149-2163
    • Arnold, S.M.1    Fessler, L.I.2    Fessler, J.H.3    Kaufman, R.J.4
  • 9
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner S, (1974) The genetics of Caenorhabditis elegans. Genetics 77: 71-94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 10
    • 0032476580 scopus 로고    scopus 로고
    • The UDP-Glc:Glycoprotein glucosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress
    • Fanchiotti S, Fernandez F, D'Alessio C, Parodi AJ, (1998) The UDP-Glc:Glycoprotein glucosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress. J Cell Biol 143: 625-635.
    • (1998) J Cell Biol , vol.143 , pp. 625-635
    • Fanchiotti, S.1    Fernandez, F.2    D'Alessio, C.3    Parodi, A.J.4
  • 11
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno S, Klar A, Nurse P, (1991) Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol 194: 795-823.
    • (1991) Methods Enzymol , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 12
    • 0038071985 scopus 로고
    • The enzymatic synthesis of uridine diphosphate (14C)-glucose
    • Wright A, Robbins PW, (1965) The enzymatic synthesis of uridine diphosphate (14C)-glucose. Biochim Biophys ACTA 104: 594-596.
    • (1965) Biochim Biophys ACTA , vol.104 , pp. 594-596
    • Wright, A.1    Robbins, P.W.2
  • 14
    • 0028150802 scopus 로고
    • Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme fro Saccharomyces cerevisiae
    • Fernandez FS, Trombetta SE, Hellman U, Parodi AJ, (1994) Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme fro Saccharomyces cerevisiae. J Biol Chem 269: 30701-30706.
    • (1994) J Biol Chem , vol.269 , pp. 30701-30706
    • Fernandez, F.S.1    Trombetta, S.E.2    Hellman, U.3    Parodi, A.J.4
  • 15
    • 0024468302 scopus 로고
    • Glucosylation of glycoproteins by mammalian, plant, fungal, and trypanosomatid protozoa microsomal membranes
    • Trombetta SE, Bosch M, Parodi AJ, (1989) Glucosylation of glycoproteins by mammalian, plant, fungal, and trypanosomatid protozoa microsomal membranes. Biochemistry 28: 8108-8116.
    • (1989) Biochemistry , vol.28 , pp. 8108-8116
    • Trombetta, S.E.1    Bosch, M.2    Parodi, A.J.3
  • 16
    • 0032578911 scopus 로고    scopus 로고
    • Specific interference by ingested dsRNA
    • Timmons L, Fire A, (1998) Specific interference by ingested dsRNA. Nature 395: 854.
    • (1998) Nature , vol.395 , pp. 854
    • Timmons, L.1    Fire, A.2
  • 17
    • 18244405070 scopus 로고    scopus 로고
    • Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development
    • Shen X, Ellis RE, Lee K, Liu CY, Yang K, et al. (2001) Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell 107: 893-903.
    • (2001) Cell , vol.107 , pp. 893-903
    • Shen, X.1    Ellis, R.E.2    Lee, K.3    Liu, C.Y.4    Yang, K.5
  • 18
    • 33745606008 scopus 로고    scopus 로고
    • Genetic interactions due to constitutive and inducible gene regulation mediated by the unfolded protein response in C. elegans
    • Shen X, Ellis RE, Sakaki K, Kaufman RJ, (2005) Genetic interactions due to constitutive and inducible gene regulation mediated by the unfolded protein response in C. elegans. PLoS Genet 1: e37.
    • (2005) PLoS Genet , vol.1
    • Shen, X.1    Ellis, R.E.2    Sakaki, K.3    Kaufman, R.J.4
  • 19
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon M, Zeng H, Urano F, Till JH, Hubbard SR, et al. (2002) IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415: 92-96.
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5
  • 20
    • 0037135986 scopus 로고    scopus 로고
    • A survival pathway for Caenorhabditis elegans with a blocked unfolded protein response
    • Urano F, Calfon M, Yoneda T, Yun C, Kiraly M, et al. (2002) A survival pathway for Caenorhabditis elegans with a blocked unfolded protein response. J Cell Biol 158: 639-646.
    • (2002) J Cell Biol , vol.158 , pp. 639-646
    • Urano, F.1    Calfon, M.2    Yoneda, T.3    Yun, C.4    Kiraly, M.5
  • 21
    • 9144228073 scopus 로고    scopus 로고
    • Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II
    • Yamamoto K, Yoshida H, Kokame K, Kaufman RJ, Mori K, (2004) Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II. J Biochem 136: 343-350.
    • (2004) J Biochem , vol.136 , pp. 343-350
    • Yamamoto, K.1    Yoshida, H.2    Kokame, K.3    Kaufman, R.J.4    Mori, K.5
  • 22
    • 46149112775 scopus 로고    scopus 로고
    • GTPase-mediated regulation of the unfolded protein response in Caenorhabditis elegans is dependent on the AAA+ ATPase CDC-48
    • Caruso ME, Jenna S, Bouchecareilh M, Baillie DL, Boismenu D, et al. (2008) GTPase-mediated regulation of the unfolded protein response in Caenorhabditis elegans is dependent on the AAA+ ATPase CDC-48. Mol Cell Biol 28: 4261-4274.
    • (2008) Mol Cell Biol , vol.28 , pp. 4261-4274
    • Caruso, M.E.1    Jenna, S.2    Bouchecareilh, M.3    Baillie, D.L.4    Boismenu, D.5
  • 24
    • 34548010305 scopus 로고    scopus 로고
    • Differential requirement of unfolded protein response pathway for calreticulin expression in Caenorhabditis elegans
    • Lee D, Singaravelu G, Park BJ, Ahnn J, (2007) Differential requirement of unfolded protein response pathway for calreticulin expression in Caenorhabditis elegans. J Mol Biol 372: 331-340.
    • (2007) J Mol Biol , vol.372 , pp. 331-340
    • Lee, D.1    Singaravelu, G.2    Park, B.J.3    Ahnn, J.4
  • 25
    • 0035163564 scopus 로고    scopus 로고
    • Calreticulin, a calcium-binding molecular chaperone, is required for stress response and fertility in Caenorhabditis elegans
    • Park BJ, Lee DG, Yu JR, Jung SK, Choi K, et al. (2001) Calreticulin, a calcium-binding molecular chaperone, is required for stress response and fertility in Caenorhabditis elegans. Mol Biol Cell 12: 2835-2845.
    • (2001) Mol Biol Cell , vol.12 , pp. 2835-2845
    • Park, B.J.1    Lee, D.G.2    Yu, J.R.3    Jung, S.K.4    Choi, K.5
  • 26
    • 27744495877 scopus 로고    scopus 로고
    • Caenorhabditis elegans calnexin is N-glycosylated and required for stress response
    • Lee W, Lee TH, Park BJ, Chang JW, Yu JR, et al. (2005) Caenorhabditis elegans calnexin is N-glycosylated and required for stress response. Biochem Biophys Res Commun 338: 1018-1030.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 1018-1030
    • Lee, W.1    Lee, T.H.2    Park, B.J.3    Chang, J.W.4    Yu, J.R.5
  • 27
    • 0036838084 scopus 로고    scopus 로고
    • Early postnatal death and motor disorders in mice congenitally deficient in calnexin expression
    • Denzel A, Molinari M, Trigueros C, Martin JE, Velmurgan S, et al. (2002) Early postnatal death and motor disorders in mice congenitally deficient in calnexin expression. Mol Cell Biol 22: 7398-7404.
    • (2002) Mol Cell Biol , vol.22 , pp. 7398-7404
    • Denzel, A.1    Molinari, M.2    Trigueros, C.3    Martin, J.E.4    Velmurgan, S.5
  • 29
    • 77953809347 scopus 로고    scopus 로고
    • ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase
    • Coe H, Michalak M, (2010) ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase. Int J Biochem Cell Biol 42: 796-799.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 796-799
    • Coe, H.1    Michalak, M.2
  • 30
    • 0035960074 scopus 로고    scopus 로고
    • Necrotic cell death in C. elegans requires the function of calreticulin and regulators of Ca(2+) release from the endoplasmic reticulum
    • Xu K, Tavernarakis N, Driscoll M, (2001) Necrotic cell death in C. elegans requires the function of calreticulin and regulators of Ca(2+) release from the endoplasmic reticulum. Neuron 31: 957-971.
    • (2001) Neuron , vol.31 , pp. 957-971
    • Xu, K.1    Tavernarakis, N.2    Driscoll, M.3
  • 31
    • 79951671303 scopus 로고    scopus 로고
    • Unfolded Protein Response (UPR) is activated during normal lens development
    • Firtina Z, Duncan MK, (2011) Unfolded Protein Response (UPR) is activated during normal lens development. Gene Expr Patterns 11: 135-143.
    • (2011) Gene Expr Patterns , vol.11 , pp. 135-143
    • Firtina, Z.1    Duncan, M.K.2
  • 32
    • 36348930605 scopus 로고    scopus 로고
    • The role of brain-derived neurotrophic factor (BDNF)-induced XBP1 splicing during brain development
    • Hayashi A, Kasahara T, Iwamoto K, Ishiwata M, Kametani M, et al. (2007) The role of brain-derived neurotrophic factor (BDNF)-induced XBP1 splicing during brain development. J Biol Chem 282: 34525-34534.
    • (2007) J Biol Chem , vol.282 , pp. 34525-34534
    • Hayashi, A.1    Kasahara, T.2    Iwamoto, K.3    Ishiwata, M.4    Kametani, M.5
  • 33
    • 0742330341 scopus 로고    scopus 로고
    • Heat shock factor functions at the convergence of the stress response and developmental pathways in Caenorhabditis elegans
    • Walker GA, Thompson FJ, Brawley A, Scanlon T, Devaney E, (2003) Heat shock factor functions at the convergence of the stress response and developmental pathways in Caenorhabditis elegans. FASEB J 17: 1960-1962.
    • (2003) FASEB J , vol.17 , pp. 1960-1962
    • Walker, G.A.1    Thompson, F.J.2    Brawley, A.3    Scanlon, T.4    Devaney, E.5
  • 34
    • 0242321979 scopus 로고    scopus 로고
    • The noncatalytic portion of human UDP-glucose: glycoprotein glucosyltransferase I confers UDP-glucose binding and transferase function to the catalytic domain
    • Arnold SM, Kaufman RJ, (2003) The noncatalytic portion of human UDP-glucose: glycoprotein glucosyltransferase I confers UDP-glucose binding and transferase function to the catalytic domain. J Biol Chem 278: 43320-43328.
    • (2003) J Biol Chem , vol.278 , pp. 43320-43328
    • Arnold, S.M.1    Kaufman, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.