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Volumn 16, Issue 4, 2004, Pages 356-363

The roles of enzyme localisation and complex formation in glycan assembly within the Golgi apparatus

Author keywords

2 O sulfotransferase; 2OST; endoplasmic reticulum; ER; GAG; galactosylceramide; galactosyltransferase 2; GalCer; GalNacT; GalT2; GlcA; GlcA transferase; GlcAT; GlcNAc; glucuronic acid; glycosylaminoglycan; N acetylgalactosaminyltransferase; N acetylglucosamine

Indexed keywords

GLYCAN; GLYCOLIPID; GLYCOSAMINOGLYCAN; GLYCOSYLTRANSFERASE;

EID: 3142514373     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2004.06.007     Document Type: Review
Times cited : (96)

References (46)
  • 2
    • 0033579467 scopus 로고    scopus 로고
    • The cytoplasmic, transmembrane, and stem regions of glycosyltransferases specify their in vivo functional sublocalization and stability in the Golgi
    • Grabenhorst E., Conradt H.S. The cytoplasmic, transmembrane, and stem regions of glycosyltransferases specify their in vivo functional sublocalization and stability in the Golgi. J Biol Chem. 274:1999;36107-36116
    • (1999) J Biol Chem , vol.274 , pp. 36107-36116
    • Grabenhorst, E.1    Conradt, H.S.2
  • 3
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman J.E., Wieland F.T. Protein sorting by transport vesicles. Science. 272:1996;227-234
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 4
    • 0032433851 scopus 로고    scopus 로고
    • The curious status of the Golgi apparatus
    • Glick B.S., Malhotra V. The curious status of the Golgi apparatus. Cell. 95:1998;883-889
    • (1998) Cell , vol.95 , pp. 883-889
    • Glick, B.S.1    Malhotra, V.2
  • 5
    • 0035945347 scopus 로고    scopus 로고
    • Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: A role for ArfGAP1
    • Lanoix J., Ouwendijk J., Stark A., Szafer E., Cassel D., Dejgaard K., Weiss M., Nilsson T. Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: a role for ArfGAP1. J Cell Biol. 155:2001;1199-1212
    • (2001) J Cell Biol , vol.155 , pp. 1199-1212
    • Lanoix, J.1    Ouwendijk, J.2    Stark, A.3    Szafer, E.4    Cassel, D.5    Dejgaard, K.6    Weiss, M.7    Nilsson, T.8
  • 6
    • 0035945348 scopus 로고    scopus 로고
    • Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport
    • Martinez-Menarguez J.A., Prekeris R., Oorschot V.M., Scheller R., Slot J.W., Geuze H.J., Klumperman J. Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport. J Cell Biol. 155:2001;1213-1224
    • (2001) J Cell Biol , vol.155 , pp. 1213-1224
    • Martinez-Menarguez, J.A.1    Prekeris, R.2    Oorschot, V.M.3    Scheller, R.4    Slot, J.W.5    Geuze, H.J.6    Klumperman, J.7
  • 8
    • 0034664730 scopus 로고    scopus 로고
    • The debate about transport in the Golgi - Two sides of the same coin?
    • Pelham H.R., Rothman J.E. The debate about transport in the Golgi - two sides of the same coin? Cell. 102:2000;713-719
    • (2000) Cell , vol.102 , pp. 713-719
    • Pelham, H.R.1    Rothman, J.E.2
  • 9
    • 0036704669 scopus 로고    scopus 로고
    • The Golgi apparatus: Balancing new with old
    • Storrie B., Nilsson T. The Golgi apparatus: balancing new with old. Traffic. 3:2002;521-529
    • (2002) Traffic , vol.3 , pp. 521-529
    • Storrie, B.1    Nilsson, T.2
  • 10
    • 0038050371 scopus 로고    scopus 로고
    • Cisternal maturation and vesicle transport: Join the band wagon!
    • Elsner M., Hashimoto H., Nilsson T. Cisternal maturation and vesicle transport: join the band wagon! Mol Membr Biol. 20:2003;221-229
    • (2003) Mol Membr Biol , vol.20 , pp. 221-229
    • Elsner, M.1    Hashimoto, H.2    Nilsson, T.3
  • 11
    • 0027318045 scopus 로고
    • Kin recognition. A model for the retention of Golgi enzymes
    • Nilsson T., Slusarewicz P., Hoe M.H., Warren G. Kin recognition. A model for the retention of Golgi enzymes. FEBS Lett. 330:1993;1-4
    • (1993) FEBS Lett , vol.330 , pp. 1-4
    • Nilsson, T.1    Slusarewicz, P.2    Hoe, M.H.3    Warren, G.4
  • 12
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher M.S., Munro S. Cholesterol and the Golgi apparatus. Science. 261:1993;1280-1281
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 13
    • 0035881822 scopus 로고    scopus 로고
    • Steady-state localization of a medial-Golgi glycosyltransferase involves transit through the trans-Golgi network
    • Opat A.S., Houghton F., Gleeson P.A. Steady-state localization of a medial-Golgi glycosyltransferase involves transit through the trans-Golgi network. Biochem J. 358:2001;33-40
    • (2001) Biochem J , vol.358 , pp. 33-40
    • Opat, A.S.1    Houghton, F.2    Gleeson, P.A.3
  • 14
    • 0034697118 scopus 로고    scopus 로고
    • Medial Golgi but not late Golgi glycosyltransferases exist as high molecular weight complexes. Role of luminal domain in complex formation and localization
    • Opat A.S., Houghton F., Gleeson P.A. Medial Golgi but not late Golgi glycosyltransferases exist as high molecular weight complexes. Role of luminal domain in complex formation and localization. J Biol Chem. 275:2000;11836-11845
    • (2000) J Biol Chem , vol.275 , pp. 11836-11845
    • Opat, A.S.1    Houghton, F.2    Gleeson, P.A.3
  • 15
    • 0031976015 scopus 로고    scopus 로고
    • Localization of proteins to the Golgi apparatus
    • Munro S. Localization of proteins to the Golgi apparatus. Trends Cell Biol. 8:1998;11-15
    • (1998) Trends Cell Biol , vol.8 , pp. 11-15
    • Munro, S.1
  • 17
    • 0029834675 scopus 로고    scopus 로고
    • Interleaflet clear space is reduced in the membrane of COP I-and COP II-coated buds/vesicles
    • Orci L., Schekman R., Perrelet A. Interleaflet clear space is reduced in the membrane of COP I-and COP II-coated buds/vesicles. Proc Natl Acad Sci USA. 93:1996;8968-8970
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8968-8970
    • Orci, L.1    Schekman, R.2    Perrelet, A.3
  • 18
    • 0039992226 scopus 로고    scopus 로고
    • Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus
    • Rottger S., White J., Wandall H.H., Olivo J.C., Stark A., Bennett E.P., Whitehouse C., Berger E.G., Clausen H., Nilsson T. Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. J Cell Sci. 111:1998;45-60
    • (1998) J Cell Sci , vol.111 , pp. 45-60
    • Rottger, S.1    White, J.2    Wandall, H.H.3    Olivo, J.C.4    Stark, A.5    Bennett, E.P.6    Whitehouse, C.7    Berger, E.G.8    Clausen, H.9    Nilsson, T.10
  • 19
    • 0036678493 scopus 로고    scopus 로고
    • Structure of the Golgi and distribution of reporter molecules at 20°C reveals the complexity of the exit compartments
    • Ladinsky M.S., Wu C.C., McIntosh S., McIntosh J.R., Howell K.E. Structure of the Golgi and distribution of reporter molecules at 20°C reveals the complexity of the exit compartments. Mol Biol Cell. 13:2002;2810-2825
    • (2002) Mol Biol Cell , vol.13 , pp. 2810-2825
    • Ladinsky, M.S.1    Wu, C.C.2    McIntosh, S.3    McIntosh, J.R.4    Howell, K.E.5
  • 21
    • 0030937062 scopus 로고    scopus 로고
    • Glycosylation: Heterogeneity and the 3D structure of proteins
    • Rudd P.M., Dwek R.A. Glycosylation: heterogeneity and the 3D structure of proteins. Crit Rev Biochem Mol Biol. 32:1997;1-100
    • (1997) Crit Rev Biochem Mol Biol , vol.32 , pp. 1-100
    • Rudd, P.M.1    Dwek, R.A.2
  • 22
    • 0035800822 scopus 로고    scopus 로고
    • Location and mechanism of α-2,6-sialyltransferase dimer formation. Role of cysteine residues in enzyme dimerization, localization, activity, and processing
    • Qian R., Chen C., Colley K.J. Location and mechanism of α-2, 6-sialyltransferase dimer formation. Role of cysteine residues in enzyme dimerization, localization, activity, and processing. J Biol Chem. 276:2001;28641-28649
    • (2001) J Biol Chem , vol.276 , pp. 28641-28649
    • Qian, R.1    Chen, C.2    Colley, K.J.3
  • 23
    • 0037470039 scopus 로고    scopus 로고
    • Importance of Cys, Gln, and Tyr from the transmembrane domain of human α3/4 fucosyltransferase III for its localization and sorting in the Golgi of baby hamster kidney cells
    • Sousa V.L., Brito C., Costa T., Lanoix J., Nilsson T., Costa J. Importance of Cys, Gln, and Tyr from the transmembrane domain of human α3/4 fucosyltransferase III for its localization and sorting in the Golgi of baby hamster kidney cells. J Biol Chem. 278:2003;7624-7629
    • (2003) J Biol Chem , vol.278 , pp. 7624-7629
    • Sousa, V.L.1    Brito, C.2    Costa, T.3    Lanoix, J.4    Nilsson, T.5    Costa, J.6
  • 24
    • 0026607683 scopus 로고
    • Golgi retention of a trans-Golgi membrane protein, galactosyltransferase, requires cysteine and histidine residues within the membrane-anchoring domain
    • Aoki D., Lee N., Yamaguchi N., Dubois C., Fukuda M.N. Golgi retention of a trans-Golgi membrane protein, galactosyltransferase, requires cysteine and histidine residues within the membrane-anchoring domain. Proc Natl Acad Sci USA. 89:1992;4319-4323
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4319-4323
    • Aoki, D.1    Lee, N.2    Yamaguchi, N.3    Dubois, C.4    Fukuda, M.N.5
  • 26
    • 0036462601 scopus 로고    scopus 로고
    • Protein N-glycosylation along the secretory pathway: Relationship to organelle topography and function, protein quality control, and cell interactions
    • Roth J. Protein N-glycosylation along the secretory pathway: relationship to organelle topography and function, protein quality control, and cell interactions. Chem Rev. 102:2002;285-303
    • (2002) Chem Rev , vol.102 , pp. 285-303
    • Roth, J.1
  • 27
    • 0029890064 scopus 로고    scopus 로고
    • The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase I in retention, kin recognition and structural maintenance of the Golgi apparatus in HeLa cells
    • Nilsson T., Rabouille C., Hui N., Watson R., Warren G. The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase I in retention, kin recognition and structural maintenance of the Golgi apparatus in HeLa cells. J Cell Sci. 109:1996;1975-1989
    • (1996) J Cell Sci , vol.109 , pp. 1975-1989
    • Nilsson, T.1    Rabouille, C.2    Hui, N.3    Watson, R.4    Warren, G.5
  • 28
    • 0035827374 scopus 로고    scopus 로고
    • What can yeast tell us about N-linked glycosylation in the Golgi apparatus?
    • Munro S. What can yeast tell us about N-linked glycosylation in the Golgi apparatus? FEBS Lett. 498:2001;223-227
    • (2001) FEBS Lett , vol.498 , pp. 223-227
    • Munro, S.1
  • 29
    • 0032518685 scopus 로고    scopus 로고
    • Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with α-1,6-mannosyltransferase activity
    • Jungmann J., Munro S. Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with α-1, 6-mannosyltransferase activity. EMBO J. 17:1998;423-434
    • (1998) EMBO J , vol.17 , pp. 423-434
    • Jungmann, J.1    Munro, S.2
  • 30
    • 0037160121 scopus 로고    scopus 로고
    • The components of the Saccharomyces cerevisiae mannosyltransferase complex M-Pol I have distinct functions in mannan synthesis
    • Stolz J., Munro S. The components of the Saccharomyces cerevisiae mannosyltransferase complex M-Pol I have distinct functions in mannan synthesis. J Biol Chem. 277:2002;44801-44808
    • (2002) J Biol Chem , vol.277 , pp. 44801-44808
    • Stolz, J.1    Munro, S.2
  • 31
    • 0033525512 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae protein Mnn10p/Bed1p is a subunit of a Golgi mannosyltransferase complex
    • Jungmann J., Rayner J.C., Munro S. The Saccharomyces cerevisiae protein Mnn10p/Bed1p is a subunit of a Golgi mannosyltransferase complex. J Biol Chem. 274:1999;6579-6585
    • (1999) J Biol Chem , vol.274 , pp. 6579-6585
    • Jungmann, J.1    Rayner, J.C.2    Munro, S.3
  • 32
    • 0035852635 scopus 로고    scopus 로고
    • Physical and functional association of glycolipid N-acetyl-galactosaminyl and galactosyl transferases in the Golgi apparatus
    • Giraudo C.G., Daniotti J.L., Maccioni H.J. Physical and functional association of glycolipid N-acetyl-galactosaminyl and galactosyl transferases in the Golgi apparatus. Proc Natl Acad Sci USA. 98:2001;1625-1630
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1625-1630
    • Giraudo, C.G.1    Daniotti, J.L.2    MacCioni, H.J.3
  • 33
    • 0141890299 scopus 로고    scopus 로고
    • Ganglioside glycosyltransferases organize in distinct multienzyme complexes in CHO-K1 cells
    • Three enzymes that function early in the glyolipid biosynthetic pathway, SialT1, GalT1, and SialT2, form a complex in the proximal Golgi. SialT1 is required for GalT1 and SialT2 to associate, suggesting that SialT1 is key to complex formation.
    • Giraudo C.G., Maccioni H.J. Ganglioside glycosyltransferases organize in distinct multienzyme complexes in CHO-K1 cells. J Biol Chem. 278:2003;40262-40271 Three enzymes that function early in the glyolipid biosynthetic pathway, SialT1, GalT1, and SialT2, form a complex in the proximal Golgi. SialT1 is required for GalT1 and SialT2 to associate, suggesting that SialT1 is key to complex formation.
    • (2003) J Biol Chem , vol.278 , pp. 40262-40271
    • Giraudo, C.G.1    MacCioni, H.J.2
  • 35
    • 0031711820 scopus 로고    scopus 로고
    • Transporters of nucleotide sugars, ATP, and nucleotide sulfate in the endoplasmic reticulum and Golgi apparatus
    • Hirschberg C.B., Robbins P.W., Abeijon C. Transporters of nucleotide sugars, ATP, and nucleotide sulfate in the endoplasmic reticulum and Golgi apparatus. Annu Rev Biochem. 67:1998;49-69
    • (1998) Annu Rev Biochem , vol.67 , pp. 49-69
    • Hirschberg, C.B.1    Robbins, P.W.2    Abeijon, C.3
  • 36
    • 0032475872 scopus 로고    scopus 로고
    • UDP-galactose:ceramide galactosyltransferase is a class I integral membrane protein of the endoplasmic reticulum
    • Sprong H., Kruithof B., Leijendekker R., Slot J.W., van Meer G., van der Sluijs P. UDP-galactose:ceramide galactosyltransferase is a class I integral membrane protein of the endoplasmic reticulum. J Biol Chem. 273:1998;25880-25888
    • (1998) J Biol Chem , vol.273 , pp. 25880-25888
    • Sprong, H.1    Kruithof, B.2    Leijendekker, R.3    Slot, J.W.4    Van Meer, G.5    Van Der Sluijs, P.6
  • 37
    • 0042970585 scopus 로고    scopus 로고
    • Association of the Golgi UDP-galactose transporter with UDP-galactose:ceramide galactosyltransferase allows UDP-galactose import in the endoplasmic reticulum
    • The UDP-galactose transporter UGT forms a complex with an ER-resident galactosyltransferase, leading to its retention in the ER and allowing the production of GalCer. To our knowledge, this is the only reported association between a sugar nucleotide transporter and a glycosyltransferase.
    • Sprong H., Degroote S., Nilsson T., Kawakita M., Ishida N., van der Sluijs P., van Meer G. Association of the Golgi UDP-galactose transporter with UDP-galactose:ceramide galactosyltransferase allows UDP-galactose import in the endoplasmic reticulum. Mol Biol Cell. 14:2003;3482-3493 The UDP-galactose transporter UGT forms a complex with an ER-resident galactosyltransferase, leading to its retention in the ER and allowing the production of GalCer. To our knowledge, this is the only reported association between a sugar nucleotide transporter and a glycosyltransferase.
    • (2003) Mol Biol Cell , vol.14 , pp. 3482-3493
    • Sprong, H.1    Degroote, S.2    Nilsson, T.3    Kawakita, M.4    Ishida, N.5    Van Der Sluijs, P.6    Van Meer, G.7
  • 38
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: Assembly of ligand binding sites in heparan sulfate
    • Esko J.D., Selleck S.B. Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu Rev Biochem. 71:2002;435-471
    • (2002) Annu Rev Biochem , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 39
    • 0032500662 scopus 로고    scopus 로고
    • The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate
    • Lind T., Tufaro F., McCormick C., Lindahl U., Lidholt K. The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. J Biol Chem. 273:1998;26265-26268
    • (1998) J Biol Chem , vol.273 , pp. 26265-26268
    • Lind, T.1    Tufaro, F.2    McCormick, C.3    Lindahl, U.4    Lidholt, K.5
  • 40
    • 0034681139 scopus 로고    scopus 로고
    • The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate
    • McCormick C., Duncan G., Goutsos K.T., Tufaro F. The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate. Proc Natl Acad Sci USA. 97:2000;668-673
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 668-673
    • McCormick, C.1    Duncan, G.2    Goutsos, K.T.3    Tufaro, F.4
  • 41
    • 0035818480 scopus 로고    scopus 로고
    • Enzyme interactions in heparan sulfate biosynthesis: Uronosyl 5-epimerase and 2-O-sulfotransferase interact in vivo
    • Pinhal M.A., Smith B., Olson S., Aikawa J., Kimata K., Esko J.D. Enzyme interactions in heparan sulfate biosynthesis: uronosyl 5-epimerase and 2-O-sulfotransferase interact in vivo. Proc Natl Acad Sci USA. 98:2001;12984-12989
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12984-12989
    • Pinhal, M.A.1    Smith, B.2    Olson, S.3    Aikawa, J.4    Kimata, K.5    Esko, J.D.6
  • 42
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc:polypeptide N- acetylgalactosaminyltransferases
    • Ten Hagen K.G., Fritz T.A., Tabak L.A. All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycobiology. 13:2003;1R-16R
    • (2003) Glycobiology , vol.13
    • Ten Hagen, K.G.1    Fritz, T.A.2    Tabak, L.A.3
  • 43
    • 0037646471 scopus 로고    scopus 로고
    • Extended core 1 and core 2 branched O-glycans differentially modulate sialyl Lewis X-type L-selectin ligand activity
    • Mitoma J., Petryniak B., Hiraoka N., Yeh J.C., Lowe J.B., Fukuda M. Extended core 1 and core 2 branched O-glycans differentially modulate sialyl Lewis X-type L-selectin ligand activity. J Biol Chem. 278:2003;9953-9961
    • (2003) J Biol Chem , vol.278 , pp. 9953-9961
    • Mitoma, J.1    Petryniak, B.2    Hiraoka, N.3    Yeh, J.C.4    Lowe, J.B.5    Fukuda, M.6
  • 44
    • 0032567431 scopus 로고    scopus 로고
    • Synthesis of poly-N-acetyllactosamine in core 2 branched O-glycans. The requirement of novel β-1,4-galactosyltransferase IV and β-1,3-N-acetylglucosaminyltransferase
    • Ujita M., McAuliffe J., Schwientek T., Almeida R., Hindsgaul O., Clausen H., Fukuda M. Synthesis of poly-N-acetyllactosamine in core 2 branched O-glycans. The requirement of novel β-1, 4-galactosyltransferase IV and β-1, 3-N-acetylglucosaminyltransferase. J Biol Chem. 273:1998;34843-34849
    • (1998) J Biol Chem , vol.273 , pp. 34843-34849
    • Ujita, M.1    McAuliffe, J.2    Schwientek, T.3    Almeida, R.4    Hindsgaul, O.5    Clausen, H.6    Fukuda, M.7
  • 45
    • 0038603867 scopus 로고    scopus 로고
    • The Golgi protein RCAS1 controls cell surface expression of tumor-associated O-linked glycan antigens
    • Originally characterised as a cell surface protein involved in apoptosis, the authors show that RCAS1 is actually a Golgi resident protein and that its overexpression leads to the truncation of O-linked glycans.
    • Engelsberg A., Hermosilla R., Karsten U., Schulein R., Dorken B., Rehm A. The Golgi protein RCAS1 controls cell surface expression of tumor-associated O-linked glycan antigens. J Biol Chem. 278:2003;22998-23007 Originally characterised as a cell surface protein involved in apoptosis, the authors show that RCAS1 is actually a Golgi resident protein and that its overexpression leads to the truncation of O-linked glycans.
    • (2003) J Biol Chem , vol.278 , pp. 22998-23007
    • Engelsberg, A.1    Hermosilla, R.2    Karsten, U.3    Schulein, R.4    Dorken, B.5    Rehm, A.6
  • 46
    • 0037168608 scopus 로고    scopus 로고
    • A unique molecular chaperone Cosmc required for activity of the mammalian core 1 β3-galactosyltransferase
    • The core 1 galactosyltransferase is vital for the production of most common O-glycans. The protein Cosmc functions as a molecular chaperone for this enzyme, thus controlling an important junction in O-linked biosynthesis. Jurkat cells have a mutation in Cosmc, leading to proteasome-mediated degradation of the galactosyltransferase, which can be prevented by complementation with the functional chaperone.
    • Ju T., Cummings R.D. A unique molecular chaperone Cosmc required for activity of the mammalian core 1 β3-galactosyltransferase. Proc Natl Acad Sci USA. 99:2002;16613-16618 The core 1 galactosyltransferase is vital for the production of most common O-glycans. The protein Cosmc functions as a molecular chaperone for this enzyme, thus controlling an important junction in O-linked biosynthesis. Jurkat cells have a mutation in Cosmc, leading to proteasome-mediated degradation of the galactosyltransferase, which can be prevented by complementation with the functional chaperone.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16613-16618
    • Ju, T.1    Cummings, R.D.2


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