Mannosidase action, independent of glucose trimming, is essential for proteasome-mediated degradation of unassembled glycosylated Ig light chains

Biological Chemistry

Volumn 381, Issue 12, 2000, Pages 1155-1164

  Chillaron J ^a   Adan C ^a   Haas, I G ^a  

^a UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

Calnexin; Calreticulin; ER mannosidases; ER associated degradation (ERAD); Short lived protein in glycoprotein ERAD; UDP:glucose glycoprotein glucosyl transferase

Indexed keywords

1 DEOXYMANNONOJIRIMYCIN; ALPHA 1 ANTITRYPSIN; CALNEXIN; CALRETICULIN; CHAPERONE; COMPLEMENTARY DNA; CYCLOHEXIMIDE; GLUCOSE; GLUCOSIDASE; GLYCAN DERIVATIVE; GLYCOPROTEIN; GLYCOSIDASE; GLYCOSIDASE INHIBITOR; GLYCOSYLATED PROTEIN; GLYCOSYLTRANSFERASE; IMMUNOGLOBULIN LIGHT CHAIN; LACTACYSTIN; LECTIN; MANNOSE; MANNOSIDASE; MANNOSIDASE INHIBITOR; N ACETYLGLUCOSAMINE; OLIGOSACCHARIDE; POLYPEPTIDE; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN SYNTHESIS INHIBITOR; PUROMYCIN; UNINDEXED DRUG; URIDINE DIPHOSPHATE GLUCOSE;

ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CONTROLLED STUDY; DRUG ACTIVITY; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INHIBITION; GENETIC TRANSFECTION; GLUCOSE METABOLISM; HELA CELL; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN PROCESSING; PROTEIN SYNTHESIS;

ANIMALS; CYSTEINE ENDOPEPTIDASES; ENDOPLASMIC RETICULUM; FABACEAE; GENES, IMMUNOGLOBULIN; GLUCOSE; GLUCOSIDASES; GLYCOSYLATION; HELA CELLS; HUMANS; IMMUNOGLOBULIN LIGHT CHAINS; IMMUNOGLOBULIN VARIABLE REGION; MANNOSIDASES; MICE; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; PLANT PROTEINS; PLANTS, MEDICINAL; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN SYNTHESIS INHIBITORS; TRANSFECTION; TRANSLOCATION, GENETIC;

MURINAE;

EID: 0034516346     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2000.143     Document Type: Article

References (64)

1. The p88 molecular chaperone is identical to the endoplasmic reticulum membrane protein, calnexin
2. Complementary DNA sequence of human amyloidogenic immunoglobulin lightchain precursors
3. Differential role of mannose and glucose trimming in the ER degradation of asialoglycoprotein receptor subunits
4. Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization
5. Role of Cue1p in ubiquitination and degradation at the ER surface
6. Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins
7. Dissociation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity
8. Structure of a monoclonal kappa chain of the V kappa IV subgroup in the kidney and plasma cells in light chain deposition disease
9. Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome
10. Removal and degradation of the free MHC class II beta chain in the endoplasmic reticulum requires proteasomes and is accelerated by BFA
11. Lactacystin, proteasome function, and cell fate
12. The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene
13. A major proportion of N-glycoproteins are transiently glucosylated in the endoplasmic reticulum
14. Rapid degradation of an unassembled immunoglobulin light chain is mediated by a serine protease and occurs in a pre-Golgi compartment
15. Modification of the T cell antigen receptor (TCR) complex by UDP-glucose:g lycoprotein glucosyltransferase. TCR folding is finalized convergent with formation of alpha beta delta epsilon gamma epsilon complexes
16. Substrate specificities of rat liver microsomal glucosidases which process glycoproteins
17. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy 3-methylglutaryl CoA reductase, an integral endoplasmic reticulum membrane protein
18. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
19. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
20. The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin
21. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
22. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome
23. The alpha chain of the T cell antigen receptor is degraded in the cytosol
24. Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
25. Selective inhibition of glycoprotein-processing enzymes. Differential inhibition of glucosidases I and II in cell culture
26. Persistence of glucose residues on core oligosaccharides prevents association of TCR alpha and TCR beta proteins with calnexin and results specifically in accelerated degradation of nascent TCR alpha proteins reticulum
27. Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the alpha-subunit of the nicotinic acetylcholine receptor
28. Rapid isolation of antigens from cells with a staphylococcal protein A-antibody adsorbent: Parameters of the interaction of antibody-antigen complexes with protein A
29. Protein degradation in the endoplasmic reticulum
30. Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat shock cognate BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum
31. Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast
32. N-glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast
33. Retention of glucose units added by the UDP-Glc:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum
34. Assembly of immunoglobulin light chains as a prerequisite for secretion: A model for oligomerization dependent subunit folding
35. Effect of VK framework-1 glycosylation on the binding affinity of lymphoma-specific murine and chimeric LL2 antibodies and its potential use as a novel conjugation site
36. Presence of alpha-D-mannosidic linkage in glyco-proteins. Liberation of d-mannose from various glycoproteins by alpha-mannosidase isolated from Jack bean meal
37. Intracellular disposal of incompletely folded human alpha(1) anti-trypsin involves release from calnexin and post translational trimming of asparagine linked oligosaccharides
38. Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome
39. Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin, and ATP
40. Inhibition of glucose trimming by castanospermine results in rapid degradation of unassembled major histocompatibility complex class I molecules
41. Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing
42. Cutting edge: Proteasome involvement in the degradation of unassembled Ig light chains
43. Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus
44. Reglucosylation of glycoproteins and quality control of glycoprotein folding in the endoplasmic reticulum of yeast cells
45. Factor VIII C2 domain missense mutations exhibit defective trafficking of biologically functional proteins
46. Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin
47. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
48. Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species
49. Degradation of a mutant secretory protein, alpha(1)-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity
50. Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase
51. N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin
52. Inhibition of invariant chain (li) calnexin interaction results in enhanced degradation of Ii but does not prevent the assembly of alpha beta li complexes
53. The pathway of US11-dependent degradation of MHC class I heavy chains involves a ubiquitin-conjugated intermediate
54. The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP
55. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
56. SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane
57. Degradation of CFTR by the ubiquitin-proteasome pathway
58. The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
59. Sec61 mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
60. Nonlysosomal, pre-Golgi degradation of unassembled asialoglycoprotein receptor sub-units: A TLCK- and TPCK-sensitive cleavage within the ER
61. HRD gene dependence of endoplasmic reticulum-associated degradation
62. 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
63. Conformation-independent binding of monoglucosylated ribonuclease B to calnexin
64. Quality control in the secretory pathway: The role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations