메뉴 건너뛰기




Volumn 68, Issue 24, 2011, Pages 4091-4100

"Add-on" domains of Drosophila β1,4-N- acetylgalactosaminyltransferase B in the stem region and its pilot protein

Author keywords

DHHC; GABPI; Glycolipid; Glycosyltransferase

Indexed keywords

BETA1,4 N ACETYLGALACTOSAMINYLTRANSFERASE B; N ACETYLGALACTOSAMINE; N ACETYLGALACTOSAMINYLTRANSFERASE; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN;

EID: 82255191912     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-011-0725-3     Document Type: Article
Times cited : (4)

References (37)
  • 2
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • doi:10.1093/bioinformatics/10.6.685
    • Claros MG, von Heijne G (1994) TopPred II: an improved software for membrane protein structure predictions. Comput Appl Biosci 10:685-686. doi:10.1093/bioinformatics/10.6.685
    • (1994) Comput Appl Biosci , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 3
    • 10044268365 scopus 로고    scopus 로고
    • On the mechanism of protein palmitoylation
    • DOI 10.1038/sj.embor.7400277
    • Dietrich LE, Ungermann C (2004) On the mechanism of protein palmitoylation. EMBO Rep 5:1053-1057. doi:10.1038/sj.embor. 7400277 (Pubitemid 39600203)
    • (2004) EMBO Reports , vol.5 , Issue.11 , pp. 1053-1057
    • Dietrich, L.E.P.1    Ungermann, C.2
  • 4
    • 57349141970 scopus 로고    scopus 로고
    • Swf1p, a member of the DHHC-CRD family of palmitoyltransferases, regulates the actin cytoskeleton and polarized secretion independently of its DHHC motif
    • doi:10.1091/mbc. E08-03-0252
    • Dighe SA, Kozminski KG (2008) Swf1p, a member of the DHHC-CRD family of palmitoyltransferases, regulates the actin cytoskeleton and polarized secretion independently of its DHHC motif. Mol Biol Cell 19:4454-4468. doi:10.1091/mbc. E08-03-0252
    • (2008) Mol Biol Cell , vol.19 , pp. 4454-4468
    • Dighe, S.A.1    Kozminski, K.G.2
  • 5
    • 0033605555 scopus 로고    scopus 로고
    • Membrane topology of the mammalian CMP-sialic acid transporter
    • DOI 10.1074/jbc.274.13.8779
    • Eckhardt M, Gotza B, Gerardy-Schahn R (1999) Membrane topology of the mammalian CMP-sialic acid transporter. J Biol Chem 274:8779-8787. doi:10.1074/jbc.274.13.8779 (Pubitemid 29164676)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.13 , pp. 8779-8787
    • Eckhardt, M.1    Gotza, B.2    Gerardy-Schahn, R.3
  • 6
    • 33746587831 scopus 로고    scopus 로고
    • Identification of Golgi-localized acyl transferases that palmitoylate and regulate endothelial nitric oxide synthase
    • DOI 10.1083/jcb.200601051
    • Fernandez-Hernando C, Fukata M, Bernatchez PN, Fukata Y, Lin MI, Bredt DS, Sessa WC (2006) Identification of Golgi-localized acyl transferases that palmitoylate and regulate endothelial nitric oxide synthase. J Cell Biol 174:369-377. doi:10.1083/jcb. 200601051 (Pubitemid 44156767)
    • (2006) Journal of Cell Biology , vol.174 , Issue.3 , pp. 369-377
    • Fernandez-Hernando, C.1    Fukata, M.2    Bernatchez, P.N.3    Fukata, Y.4    Lin, M.I.5    Bredt, D.S.6    Sessa, W.C.7
  • 8
    • 65649108966 scopus 로고    scopus 로고
    • The hydrophobic cysteine-rich domain of SNAP25 couples with downstream residues to mediate membrane interactions and recognition by DHHC palmitoyl transferases
    • doi:10.1091/mbc. E08-08-0880
    • Greaves J, Prescott GR, Fukata Y, Fukata M, Salaun C, Chamberlain LH (2009) The hydrophobic cysteine-rich domain of SNAP25 couples with downstream residues to mediate membrane interactions and recognition by DHHC palmitoyl transferases. Mol Biol Cell 20:1845-1854. doi:10.1091/mbc. E08-08-0880
    • (2009) Mol Biol Cell , vol.20 , pp. 1845-1854
    • Greaves, J.1    Prescott, G.R.2    Fukata, Y.3    Fukata, M.4    Salaun, C.5    Chamberlain, L.H.6
  • 9
    • 22444448589 scopus 로고    scopus 로고
    • Functional analysis of Drosophila β1,4-N- acetlygalactosaminyltransferases
    • DOI 10.1093/glycob/cwi017
    • Haines N, Irvine KD (2005) Functional analysis of Drosophila β1, 4-N-acetlygalactosaminyltransferases. Glycobiology 15:335-346. doi:10.1093/glycob/cwi017 (Pubitemid 41214164)
    • (2005) Glycobiology , vol.15 , Issue.4 , pp. 335-346
    • Haines, N.1    Irvine, K.D.2
  • 10
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • DOI 10.1016/0378-1119(89)90358-2
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR (1989) Sitedirected mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59. doi:10.1016/0378-1119 (89) 90358-2 (Pubitemid 19125653)
    • (1989) Gene , vol.77 , Issue.1 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 11
    • 59849114984 scopus 로고    scopus 로고
    • Golgi targeting of Drosophila melanogaster β4GalNAcTB requires a DHHC protein family-related protein as a pilot
    • doi:10.1083/jcb.200801071
    • Johswich A, Kraft B, Wuhrer M, Berger M, Deelder AM, Hokke CH, Gerardy-Schahn R, Bakker H (2009) Golgi targeting of Drosophila melanogaster β4GalNAcTB requires a DHHC protein family-related protein as a pilot. J Cell Biol 184:173-183. doi:10.1083/jcb.200801071
    • (2009) J Cell Biol , vol.184 , pp. 173-183
    • Johswich, A.1    Kraft, B.2    Wuhrer, M.3    Berger, M.4    Deelder, A.M.5    Hokke, C.H.6    Gerardy-Schahn, R.7    Bakker, H.8
  • 12
    • 0021795728 scopus 로고
    • Studies with digitonin-treated rat hepatocytes (nude cells)
    • DOI 10.1002/jcb.240280304
    • Katz J, Wals PA (1985) Studies with digitonin-treated rat hepatocytes (nude cells). J Cell Biochem 28:207-228. doi:10.1002/jcb.240280304 (Pubitemid 15058716)
    • (1985) Journal of Cellular Biochemistry , vol.28 , Issue.3 , pp. 207-228
    • Katz, J.1    Wals, P.A.2
  • 13
    • 33646795021 scopus 로고    scopus 로고
    • Structural Basis of Carbohydrate Transfer Activity by Human UDP-GalNAc: Polypeptide α-N-Acetylgalactosaminyltransferase (pp-GalNAc-T10)
    • DOI 10.1016/j.jmb.2006.03.061, PII S0022283606004244
    • Kubota T, Shiba T, Sugioka S, Furukawa S, Sawaki H, Kato R, Wakatsuki S, Narimatsu H (2006) Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide α-N-acetylgalactosaminyltransferase (pp-GalNAc-T10). J Mol Biol 359:708-727. doi:10.1016/j.jmb.2006.03.061 (Pubitemid 43767270)
    • (2006) Journal of Molecular Biology , vol.359 , Issue.3 , pp. 708-727
    • Kubota, T.1    Shiba, T.2    Sugioka, S.3    Furukawa, S.4    Sawaki, H.5    Kato, R.6    Wakatsuki, S.7    Narimatsu, H.8
  • 14
    • 78651234929 scopus 로고    scopus 로고
    • Involvement of murine β-1, 4-galactosyltransferase V in lactosylceramide biosynthesis
    • doi:10.1007/s10719-010-9313-2
    • Kumagai T, Sato T, Natsuka S, Kobayashi Y, Zhou D, Shinkai T, Hayakawa S, Furukawa K (2010) Involvement of murine β-1, 4-galactosyltransferase V in lactosylceramide biosynthesis. Glycoconj J 27:685-695. doi:10.1007/s10719-010- 9313-2
    • (2010) Glycoconj J , vol.27 , pp. 685-695
    • Kumagai, T.1    Sato, T.2    Natsuka, S.3    Kobayashi, Y.4    Zhou, D.5    Shinkai, T.6    Hayakawa, S.7    Furukawa, K.8
  • 15
    • 33845794047 scopus 로고    scopus 로고
    • Palmitoylation: Policing protein stability and traffic
    • DOI 10.1038/nrm2084, PII NRM2084
    • Linder ME, Deschenes RJ (2007) Palmitoylation: policing protein stability and traffic. Nat Rev Mol Cell Biol 8:74-84. doi: 10.1038/nrm2084 (Pubitemid 46012016)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.1 , pp. 74-84
    • Linder, M.E.1    Deschenes, R.J.2
  • 16
    • 0037174987 scopus 로고    scopus 로고
    • Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M206573200
    • Lobo S, Greentree WK, Linder ME, Deschenes RJ (2002) Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. J Biol Chem 277:41268-41273. doi:10.1074/jbc. M206573200 (Pubitemid 35215719)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 41268-41273
    • Lobo, S.1    Greentree, W.K.2    Linder, M.E.3    Deschenes, R.J.4
  • 17
    • 78649662343 scopus 로고    scopus 로고
    • Mutational analysis of Saccharomyces cerevisiae Erf2 reveals a two-step reaction mechanism for protein palmitoylation by DHHC enzymes
    • doi:10.1074/jbc. M110.169102
    • Mitchell DA, Mitchell G, Ling Y, Budde C, Deschenes RJ (2010) Mutational analysis of Saccharomyces cerevisiae Erf2 reveals a two-step reaction mechanism for protein palmitoylation by DHHC enzymes. J Biol Chem 285:38104-38114. doi:10.1074/jbc. M110.169102
    • (2010) J Biol Chem , vol.285 , pp. 38104-38114
    • Mitchell, D.A.1    Mitchell, G.2    Ling, Y.3    Budde, C.4    Deschenes, R.J.5
  • 18
    • 33744826797 scopus 로고    scopus 로고
    • Protein palmitoylation by a family of DHHC protein S-acyltransferases
    • DOI 10.1194/jlr.R600007-JLR200
    • Mitchell DA, Vasudevan A, Linder ME, Deschenes RJ (2006) Protein palmitoylation by a family of DHHC protein S-acyltransferases. J Lipid Res 47:1118-1127. doi:10.1194/jlr. R600007-JLR200 (Pubitemid 43830703)
    • (2006) Journal of Lipid Research , vol.47 , Issue.6 , pp. 1118-1127
    • Mitchell, D.A.1    Vasudevan, A.2    Linder, M.E.3    Deschenes, R.J.4
  • 19
    • 77956520108 scopus 로고    scopus 로고
    • β4-galactosyltransferase-5 is a lactosylceramide synthase essential for mouse extra-embryonic development
    • doi:10.1093/glycob/cwq098
    • Nishie T, Hikimochi Y, Zama K, Fukusumi Y, Ito M, Yokoyama H, Naruse C, Ito M, Asano M (2010) β4-galactosyltransferase-5 is a lactosylceramide synthase essential for mouse extra-embryonic development. Glycobiology 20:1311-1322. doi:10.1093/glycob/cwq098
    • (2010) Glycobiology , vol.20 , pp. 1311-1322
    • Nishie, T.1    Hikimochi, Y.2    Zama, K.3    Fukusumi, Y.4    Ito, M.5    Yokoyama, H.6    Naruse, C.7    Ito, M.8    Asano, M.9
  • 21
    • 15044343147 scopus 로고    scopus 로고
    • Transmembrane topology of the protein palmitoyl transferase Akr1
    • DOI 10.1074/jbc.M411946200
    • Politis EG, Roth AF, Davis NG (2005) Transmembrane topology of the protein palmitoyl transferase Akr1. J Biol Chem 280:10156-10163. doi:10.1074/jbc. M411946200 (Pubitemid 40395869)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.11 , pp. 10156-10163
    • Politis, E.G.1    Roth, A.F.2    Davis, N.G.3
  • 22
    • 0033012819 scopus 로고    scopus 로고
    • The DHHC domain: A new highly conserved cysteine-rich motif
    • DOI 10.1023/A:1006932522197
    • Putilina T, Wong P, Gentleman S (1999) The DHHC domain: a new highly conserved cysteine-rich motif. Mol Cell Biochem 195:219-226. doi:10.1023/A:1006932522197 (Pubitemid 29259786)
    • (1999) Molecular and Cellular Biochemistry , vol.195 , Issue.1-2 , pp. 219-226
    • Putilina, T.1    Wong, P.2    Gentleman, S.3
  • 23
    • 34447305187 scopus 로고    scopus 로고
    • Letter to the glyco-forum: Catalytic domains of glycosyltransferases with 'add-on' domains
    • DOI 10.1093/glycob/cwm013
    • Qasba PK, Ramakrishnan B (2007) Letter to the Glyco-Forum: catalytic domains of glycosyltransferases with 'add-on' domains. Glycobiology 17:7G-9G. doi:10.1093/glycob/cwm013 (Pubitemid 47049933)
    • (2007) Glycobiology , vol.17 , Issue.5
    • Qasba, P.K.1    Ramakrishnan, B.2
  • 24
    • 42949090427 scopus 로고    scopus 로고
    • Structure and function of β-1,4-galactosyltransferase
    • DOI 10.2174/138945008783954943
    • Qasba PK, Ramakrishnan B, Boeggeman E (2008) Structure and function of β-1, 4-galactosyltransferase. Curr Drug Targets 9:292-309. doi:10.2174/138945008783954943 (Pubitemid 351836430)
    • (2008) Current Drug Targets , vol.9 , Issue.4 , pp. 292-309
    • Qasba, P.K.1    Ramakrishnan, B.2    Boeggeman, E.3
  • 25
    • 0036291319 scopus 로고    scopus 로고
    • Breakthroughs and views: β-1,4-galactosyltransferase and lactose synthase: Molecular mechanical devices
    • DOI 10.1006/bbrc.2002.6506
    • Ramakrishnan B, Boeggeman E, Qasba PK (2002) β-1, 4-galactosyltransferase and lactose synthase: molecular mechanical devices. Biochem Biophys Res Commun 291:1113-1118. doi: 10.1006/bbrc.2002.6506 (Pubitemid 34694303)
    • (2002) Biochemical and Biophysical Research Communications , vol.291 , Issue.5 , pp. 1113-1118
    • Ramakrishnan, B.1    Boeggeman, E.2    Qasba, P.K.3
  • 26
    • 0035813137 scopus 로고    scopus 로고
    • A-Lactalbumin (LA) stimulates milk β-1, 4-galactosyltransferase I (β4Gal-T1) to transfer glucose from UDP-glucose to N-acetylglucosamine. Crystal structure of β4Gal-T1 x LA complex with UDP-Glc
    • doi:10.1074/jbc. M102458200
    • Ramakrishnan B, Shah PS, Qasba PK (2001) a-Lactalbumin (LA) stimulates milk β-1, 4-galactosyltransferase I (β4Gal-T1) to transfer glucose from UDP-glucose to N-acetylglucosamine. Crystal structure of β4Gal-T1 x LA complex with UDP-Glc. J Biol Chem 276:37665-37671. doi:10.1074/jbc. M102458200
    • (2001) J Biol Chem , vol.276 , pp. 37665-37671
    • Ramakrishnan, B.1    Shah, P.S.2    Qasba, P.K.3
  • 27
    • 0037078323 scopus 로고    scopus 로고
    • The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase
    • DOI 10.1083/jcb.200206120
    • Roth AF, Feng Y, Chen L, Davis NG (2002) The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase. J Cell Biol 159:23-28. doi:10.1083/jcb.200206120 (Pubitemid 35191514)
    • (2002) Journal of Cell Biology , vol.159 , Issue.1 , pp. 23-28
    • Roth, A.F.1    Feng, Y.2    Chen, L.3    Davis, N.G.4
  • 29
    • 0001797804 scopus 로고    scopus 로고
    • Involvement of recombinant human β1, 4-galactosyltransferase V in lactosylceramide biosynthesis
    • Sato T, Guo S, Furukawa K (2000) Involvement of recombinant human β1, 4-galactosyltransferase V in lactosylceramide biosynthesis. Res Commun Biochem Cell Molec Biol 4:3-10
    • (2000) Res Commun Biochem Cell Molec Biol , vol.4 , pp. 3-10
    • Sato, T.1    Guo, S.2    Furukawa, K.3
  • 31
    • 0014050598 scopus 로고
    • Transient holes in the erythrocyte membrane during hypotonic hemolysis and stable holes in the membrane after lysis by saponin and lysolecithin
    • doi: 10.1083/jcb.32.1.55
    • Seeman P (1967) Transient holes in the erythrocyte membrane during hypotonic hemolysis and stable holes in the membrane after lysis by saponin and lysolecithin. J Cell Biol 32:55-70. doi: 10.1083/jcb.32.1.55
    • (1967) J Cell Biol , vol.32 , pp. 55-70
    • Seeman, P.1
  • 32
    • 51049123096 scopus 로고    scopus 로고
    • DHHC2 affects palmitoylation, stability, and functions of tetraspanins CD9 and CD151
    • doi:10.1091/mbc. E07-11-1164
    • Sharma C, Yang XH, Hemler ME (2008) DHHC2 affects palmitoylation, stability, and functions of tetraspanins CD9 and CD151. Mol Biol Cell 19:3415-3425. doi:10.1091/mbc. E07-11-1164
    • (2008) Mol Biol Cell , vol.19 , pp. 3415-3425
    • Sharma, C.1    Yang, X.H.2    Hemler, M.E.3
  • 33
    • 33745885289 scopus 로고    scopus 로고
    • Tyramide signal amplification for DNA and mRNA in situ hybridization
    • doi:10.1385/1-59745-007-3:33
    • Speel EJ, Hopman AH, Komminoth P (2006) Tyramide signal amplification for DNA and mRNA in situ hybridization. Methods Mol Biol 326:33-60. doi:10.1385/1-59745-007-3:33
    • (2006) Methods Mol Biol , vol.326 , pp. 33-60
    • Speel, E.J.1    Hopman, A.H.2    Komminoth, P.3
  • 34
    • 0034595848 scopus 로고    scopus 로고
    • Cloning and expression of the histo-blood group P(k) UDP-galactose: Galβ1-4Glcβ1-Cer α1,4-galactosyltransferase. Molecular genetic basis of the p phenotype
    • DOI 10.1074/jbc.M000728200
    • Steffensen R, Carlier K, Wiels J, Levery SB, Stroud M, Cedergren B, Nilsson SB, Bennett EP, Jersild C, Clausen H (2000) Cloning and expression of the histo-blood group Pk UDP-galactose: Galβ-4Glcβ1-cer α1, 4-galactosyltransferase. Molecular genetic basis of the p phenotype. J Biol Chem 275:16723-16729. doi:10.1074/jbc. M000728200 (Pubitemid 30398903)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 16723-16729
    • Steffensen, R.1    Carlier, K.2    Wiels, J.3    Levery, S.B.4    Stroud, M.5    Cedergren, B.6    Sojka, B.N.7    Bennett, E.P.8    Jersild, C.9    Clausen, H.10
  • 36
    • 73749085462 scopus 로고    scopus 로고
    • Localization of Golgi-resident glycosyltransferases
    • doi:10.1007/s00018-009-0126-z
    • Tu L, Banfield DK (2010) Localization of Golgi-resident glycosyltransferases. Cell Mol Life Sci 67:29-41. doi:10.1007/s00018-009-0126-z
    • (2010) Cell Mol Life Sci , vol.67 , pp. 29-41
    • Tu, L.1    Banfield, D.K.2
  • 37
    • 0034045731 scopus 로고    scopus 로고
    • Various stages of Schistosoma express Lewis(x), LacdiNAc, GalNAcβ1-4 (Fucα1-3)GlcNAc and GalNAcβ1-4(Fucα1-2Fucα1-3)GlcNAc carbohydrate epitopes: Detection with monoclonal antibodies that are characterized by enzymatically synthesized neoglycoproteins
    • van Remoortere A, Hokke CH, van Dam GJ, van Die I, Deelder AM, van den Eijnden DH (2000) Various stages of schistosoma express Lewis (x), LacdiNAc, GalNAcβ1-4 (Fucα1-3) GlcNAc and GalNAcβ1-4 (Fucα1- 2Fucα1-3) GlcNAc carbohydrate epitopes: detection with monoclonal antibodies that are characterized by enzymatically synthesized neoglycoproteins. Glycobiology 10:601-609. doi:10.1093/glycob/10.6.601 (Pubitemid 30398415)
    • (2000) Glycobiology , vol.10 , Issue.6 , pp. 601-609
    • Van Remoortere, A.1    Hokke, C.H.2    Van Dam, G.J.3    Van Die, I.4    Deelder, A.M.5    Van Den Eijnden, D.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.