N-glycan processing and glycoprotein folding

Advances in Protein Chemistry

Volumn 59, Issue , 2001, Pages 303-344

  Trombetta, E Sergio ^a   Parodi, Armando J ^a  

^a INSTITUTO DE INVESTIGACIONES BIOTECNOLÓGICAS   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CALRETICULIN; CARBOHYDRATE; CHAPERONE; GLUCOSYLTRANSFERASE; GLYCAN; GLYCOPROTEIN; LECTIN; LIPID; MANNOSIDASE; OLIGOSACCHARIDE; PROTEASOME; URIDINE DIPHOSPHATE GLUCOSE;

BIOGENESIS; COVALENT BOND; ENDOPLASMIC RETICULUM; GLYCOSYLATION; GOLGI COMPLEX; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW;

EID: 0035716912     PISSN: 00653233     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0065-3233(01)59010-5     Document Type: Review

References (173)

1. The role of lipid intermediates in the glycosylation of proteins in the eukaryotic cell
2. Synthesis and processing of asparagine-linked oligosaccharides
3. Assembly of asparagine-linked oligosaccharides
4. N-Glycosylation in trypanosomatid protozoa
5. Tetrahymena pyriformis cells are deficient in all mannose-P-dolichol-dependent mannosyltransferases but not in mannose-P-dolichol synthesis
6. Glycosylation of proteins in the protozoon Euglena gracilis
7. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
8. Competition between folding and glycosylation in the endoplasmic reticulum
9. Comparative rates of transfer of lipid-linked oligosaccharides to endogenous glycoprotein acceptors in vitro
10. A mutation that prevents glucosylation of the lipid-linked oligosaccharide precursor leads to underglycosylation of secreted yeast invertase
11. Glucosidase I, a transmembrane endoplasmic reticular glycoprotein with a luminal catalytic domain
12. Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit
13. Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein folding
14. Demonstration that a kifunensin-resistant α-mannosidase with a processing action on N-linked oligosaccharides occurs in rat liver endoplasmic reticulum and various cultured cells
15. 9GlcNAc
16. 273 to Leu alters the specificity of the yeast N-glycan processing class I α1,2-mannosidase
17. Glycoprotein synthesis in yeast. Early events in N-oligosaccharide processing in Schizosaccharomyces pombe
18. Protein glycosylation in Trypanosoma cruzi. The mechanism of glycosylation and structure of protein-bound oligosaccharides
19. 2 in calf thyroid slices: A possible recognition signal in the processing of glycoproteins
20. 2 occurs in rat liver and Phaseolus vulgaris cells
21. Glucosylation of glycoproteins by mammalian, plant, fungal and trypanosomatid protozoa microsomal proteins
22. Purification to homogeneity of UDP-Glc:Glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae
23. Genetic tailoring of N-linked oligosaccharides: The role of glucose residues in glycoprotein processing in Saccharomyces cerevisiae in vivo
24. Characterization of dolichol diphosphate oligosaccharide: Protein oligosaccharyltransferase and glycoprotein-processing glucosidases occurring in trypanosomatid protozoa
25. Phylogenetic survey of endomannosidase indicates late evolutionary appearance of this N-linked oligosaccharide processing enzyme
26. Protein glycosylation in Trypanosoma cruzi. II. Partial characterization of protein-bound oligosaccharides labeled "in vivo"
27. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:Glycoprotein glucosyltransferase
28. A major proportion of N-glycoproteins are transiently glucosylated in the endoplasmic reticulum
29. Lysosomal enzyme phosphorylation. Recognition of a protein-dependent determinant allows specific phosphorylation of oligosaccharides present on lysosomal enzymes
30. A pituitary N-acetylgalactosamine transferase that specifically recognizes glycoprotein hormones
31. The UDP-Glc:Glycoprotein glucosytransferase is a soluble protein of the endoplasmic reticulum
32. Purification to apparent homogeneity and partial characterization of rat liver UDP-Glc:Glycoprotein glucosyltransferase
33. Drosophila UDP-Glc:Glycoprotein glucosyltransferase: Sequence and characterization of an enzyme that distinguishes between denatured and native proteins
34. Topography of glycosylation reactions in the rough endoplasmic reticulum membrane
35. Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: Identification of a nucleoside diphosphatase in the endoplasmic reticulum
36. Topography of glycosylation reactions in the endoplasmic reticulum
37. The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding
38. Substrate specificities of rat liver microsomal glucosidases which process glycoproteins
39. A new stress protein: Synthesis of Schizosaccharomyces pombe UDP-Glc:Glycoprotein glucosyltransferase mRNA is induced under stress conditions but the enzyme is not essential for cell viability
40. Cloning and characterization of mammalian UDP-glucose:Glycoprotein glucosyltransferase and the development of a specific substrate for this enzyme
41. Two homologues encoding human UDP-glucose:Glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity
42. The yeast KRE5 gene encodes a probable endoplasmic reticulum protein required for (1-6)-β-glucan synthesis and normal growth
43. The UDP-Glc:Glycoprotein glucosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress
44. Molecular chaperone functions of heat-shock proteins
45. Uridine diphosphate-glucose transport into the endoplasmic reticulum of Saccharomyces cerevisiae: In vivo and in vitro evidence
46. The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:Glycoprotein glucosyltransferase
47. X-Ray structure of the soybean agglutinin cross-linked with a biantennary analog of the blood group I carbohydrate antigen
48. Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum
49. The Hsp70 and Hsp60 chaperone machines
50. The interaction of the UDP-Glc:Glycoprotein glucosyltransferase with the acceptor glycoprotein
51. Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:Glycoprotein glucosyltransferase
52. N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin
53. Post-translational protein modification in the endoplasmic reticulum. Demonstration of fatty acylase and deoxymannojirimycin-sensitive alpha-mannosidase activities
54. Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatis virus G proteins
55. Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells
56. Quality control in the endoplasmic reticulum: Folding and misfolding of vesicular stomatitis virus G protein in cells and in vitro
57. Trypanosoma cruzi calreticulin is a lectin that binds monoglucosylated oligosaccharides but not protein moieties of glycoproteins
58. A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:Glycoprotein glucosyltransferase
59. ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together
60. Retrograde protein translocation: ERADication of secretory proteins in health and disease
61. Ubiquitin and the control of protein fate in the secretory and endocytic pathways
62. Protein oligomerization in the endoplasmic reticulum
63. Setting the standards: Quality control in the secretory pathway
64. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase
65. The gene for a novel protein, a member of the protein disulfide isomerase/form I phophoinositide-specific phospholipase C family, is amplified in hydroxyrea-resistant cells
66. Molecular cloning and characterization of a cDNA for bovine phospholipase G-α: Proposal of redesignation of phopholipase C-α
67. Immunoglobulin heavy chain binding protein
68. The glucose-regulated protein grp94 is related to heat shock protein hsp90
69. The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin
70. The endoplasmic reticulum as a protein folding compartment
71. 2+ store: A view from the lumen
72. Calnexin: A molecular chaperone with a taste for carbohydrate
73. Calnexin: A membrane-bound chaperone of the endoplasmic reticulum
74. Calreticulin: One protein, one gene, many functions
75. Human, mouse, and rat calnexin cDNA cloning: Identification of potential calcium binding motifs and gene localization to human chromosome 5
76. Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
77. Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
78. Association of folding intermediates of glycoproteins with calnexin during protein maturation
79. Participation of a novel 88-kDa protein in the biogenesis of murine class I histocompatibility molecules
80. Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly
81. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
82. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
83. Calreticulin is a lectin-like molecular chaperone for glycoproteins of the endoplasmic reticulum
84. Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
85. Calreticulin interacts with newly synthesized human immunodeficiency virus Type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin
86. Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms
87. The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
88. Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules
89. Unique expression of major histocompatibility complex class I proteins in the absence of glucose trimming and calnexin association
90. Calnexin associates exclusively with individual CD3δ and T cell antigen receptor (TCR)α proteins containing incompletely trimmed glycans that are not assembled into multisubunit TCR complexes
91. Persistence of glucose residues on core oligosaccharides prevents association of TCRα and TCRβ proteins with calnexin and results specifically in accelerated degradation of nascent TCRα proteins within the endoplasmic reticulum
92. Calnexin-dependent enhancement of nicotinic acetylcholine receptor assembly and surface expression
93. Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the α-subunit of the nicotinic acetylcholine receptor
94. Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization
95. Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin
96. Promotion of tyrosinase folding in COS 7 cells by calnexin
97. Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3)
98. Truncated N-glycans affect protein folding in the ER of CHO-derived mutant cell lines without preventing calnexin binding
99. Calnexin, calreticulin and the folding of glycoproteins
100. Lectins as chaperones in glycoprotein folding
101. Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin
102. Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines
103. 2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
104. Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi
105. 2) substrate
106. Conformation independent binding of monoglucosylated ribonuclease B to calnexin
107. Distinct patterns of folding and interactions with calnexin and calreticulin in human class I MHC proteins with altered N-glycosylation
108. Glycan-dependent and-independent association of vesicular stomatitis virus G protein with calnexin
109. Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control
110. Functional relationship between calreticulin, calnexin and the ER luminal domain of calnexin
111. The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin
112. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
113. Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I
114. Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes
115. Evidence for successive peptide binding and quality control stages during MHC class I assembly
116. The related molecular chaperones calnexin and calreticulin differentially associate with nascent T cell antigen receptor proteins within the endoplasmic reticulum
117. Retention of glucose residues added by the UDP-Glc:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum
118. Quality control in the secretory pathway: The role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations
119. Assembly, sorting and exit of oligomeric proteins from the endoplasmic reticulum
120. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
121. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
122. The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins
123. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin
124. The role of ERp57 in disulfide bond formation during the assembly of major histocompatibility complex class I in a synchronized semipermeabilized cell translation system
125. The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
126. ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly
127. A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
128. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
129. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
130. Glycoprotein folding in the endoplasmic reticulum: A tale of three chaperones?
131. Molecular requirements for the interaction of class II major histocompatibility complex and invariant chain with calnexin
132. + thymocytes
133. Aglycosylated and phosphatidylinositol-anchored MHC class I molecules are associated with calnexin. Evidence implicating the class I-connecting peptide segment in calnexin association
134. The nonglycosylated glycoprotein of vesicular stomatitis virus is temperature sensitive and undergoes intracellular aggregation at elevated temperatures
135. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)
136. Retention of unassembled components of integral membrane proteins by calnexin
137. Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro
138. Calreticulin functions in vitro as a molecular chaperone for both glycosylated and nonglycosylated proteins
139. A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in α-glucosidase I
140. A lectin-resistant mouse lymphoma cell line is deficient in glucosidase II, a glycoprotein processing enzyme
141. Folding of VSV-G protein: Sequential interaction with BiP and calnexin
142. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
143. A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-kappa B
144. MHC Class I expression and transport in a calnexin-deficient cell line
145. Calreticulin is essential for cardiac development
146. The putative chaperone calmegin is required for sperm fertility
147. Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidases
148. N-Butyldeoxynojirimycin-mediated inhibition of human immunodeficiency virus entry correlates with changes in antibody recognition of the V1-V2 region of gp 120
149. Inhibition of N-glycan processing in B16 melanoma cells results in inactivation of tyrosinase but does not prevent its transport to the melanosome
150. Hepatitis B virus (HBV) envelope glycoproteins vary drastically in their sensitivity to glycan processing: Evidence that alteration of a single N-linked glycosylation site can regulate HBV secretion
151. Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide:N-glycanase activity
152. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
153. The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61α and a cytosolic, deglycosylated intermediary
154. Transfer of free polymannose-type oligosaccharides from the cytosol to lysosomes in cultured human hepatocellular carcinoma HEPG2 cells
155. Cytosol-to-lysosome transport of free polymannose-type oligosaccharides. Kinetic and specificity studies using rat liver lysosomes
156. Inhibition of invariant chain (1i)-calnexin interaction results in enhanced degradation of 1i but does not prevent the assembly of alfa beta 1i complexes
157. Differential role of mannose and glucose trimming in the ER degradation of asialoglycoprotein receptor subunits
158. Pre-Golgi degradation of yeast prepro-factor expressed in a mammalian cell. Influence of cell type-specific oligosaccharide processing on intracellular fate
159. Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: The role of N-linked glycans and the unfolded protein response
160. Glucosidase and mannosidase inhibitors mediate increased secretion of mutant_1-antitrypsin Z
161. Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome
162. Novel aspects of degradation of T Cell receptor subunits from the endoplasmic reticulum (ER) in T cells: Importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes
163. Pivotal role of calnexin and mannose trimming in regulating the endoplasmic reticulium-associated degradation of major histocompatibility complex class I heavy chain
164. Mannose trimming targets mutant α2-plasmin inhibitor for degradation by the proteasome
165. Inhibition of glucose trimming by castanospermine results in rapid degradation of unassembled major histocompatibility complex class I molecules
166. Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
167. N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase Yscy in yeast
168. Processing by endoplasmic reticulum mannosidases partitions a secretion-impaired glycoprotein into distinct disposal pathways
169. A pathway for targeting soluble misfolded proteins to the yeast vacuole
170. Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae
171. Degradation of human thyoperoxidase in the endoplasmic reticulum involves two different pathways depending on the folding state of the protein
172. Studies on degradative mechanisms mediating post-translational fragmentation of apolipoprotein B and the generation of the 70-kDa fragment
173. Tyrosinase folding and copper loading in vivo: A crucial role for calnexin and-glucosidase II