Comparative efficiencies of C-terminal signals of native glycophosphatidylinositol (GPI)-anchored proproteins in conferring GPI-anchoring

Journal of Cellular Biochemistry

Volumn 84, Issue 1, 2002, Pages 68-83

  Chen, Rui ^a   Knez, Jansen J ^a   Merrick, William C ^a   Edward Medof, M ^a  

^a CASE WESTERN RESERVE UNIVERSITY   (United States)

Author keywords

Cell surface engineering; GPI anchor; Native GPI proteins; Posttranslational processing

Indexed keywords

ALKALINE PHOSPHATASE; AMINO ACID; GLYCOSYLPHOSPHATIDYLINOSITOL; PROTEIN PRECURSOR;

AMIDATION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CHIMERA; CONTROLLED STUDY; GENETIC ENGINEERING; HUMAN; HUMAN CELL; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PROCESSING; SIGNAL TRANSDUCTION;

EID: 0035181218     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcb.1267     Document Type: Article

References (49)

1. Phosphatidylinositol-glycan (PI-G)- anchored membrane proteins: Requirement of ATP and GTP for translation-independent COOH-terminal processing
2. Yeast Gpi8p is essential for GPI anchor attachment onto proteins
3. Probing the signal for glycophosphatidylinositol anchor attachment using decay accelerating factor as a model system
4. A defect in glycophosphatidylinositol (GPI) surface proteins
5. Mammalian glycophosphatidylinositol anchor transfer to proteins and posttransfer deacylation
6. Molecular basis of the heterogeneity of expression of glycosyl phosphatidylinositol anchored proteins in paroxysmal nocturnal hemoglobinuria
7. Glycerolphosphoinositide anchors for membrane-tethering proteins
8. Phosphatidylinositol glycan (PI-G) anchored membrane proteins: Amino acid requirements adjacent to the site of cleavage, and PI-G attachment in the COOH-terminal signal peptide
9. Yeast Gaalp is required for attachment of a completed GPI anchor onto proteins
10. Molecular cloning of human homolog of yeast GAA1 which is required for attachment of glycophosphatidylinositols to proproteins
11. Cloning of murine glycosyl phosphatidylinositol anchor attachment protein, GPAA1
12. Characterization of putative glycoinositol phospholipid anchor precursors in mammalian cells. Localization of phosphoethanolamine
13. Synthesis of mannosylglucosaminylinositol phospholipids in normal but not paroxysmal nocturnal hemoglobinuria cells
14. GPI-anchors and cell membrances: A special relationship
15. Site-directed mutagenesis and epitope-mapped monoclonal antibodies define a catalytically important conformational difference between human placental and germ cell alkaline phosphatase
16. Biosynthesis of phosphatidylinositol glycan-anchored membrane proteins. Design of a simple protein substrated to characterize the enzyme that cleaves the COOH-terminal signal peptide
17. Biosynthesis of phosphatidylinositol-glycan(PI-G)-anchored membrane proteins in cell-free systems: Cleavage of the nascent protein and addition of the PI-G moiety depend on the sixe of the COOH-terminal signal peptide
18. Processing of nascent proteins to glycosylphosphatidylinositol-anchored forms in cell-free systems
19. Translation inhibition by an mRNA coding region secondary structure is determined by its proximity to the AUG initiation codon
20. Cleavage without anchor addition accompanies the processing of a nascent protein to its glycosylphosphatidylinositol-anchored form
21. The cytoplasmic extension as a determinant for glycoinositolphospholipid anchor substitution
22. Cell surface engineering with GPI-anchored proteins
23. Selectivity at the cleavage/attachment site of phosphatidylinositol-glycan anchored membrane proteins is enzymatically determined
24. Glycoinositol phospholipid anchor defective K562 mutants with biochemical lesions distinct from those in Thy-1-negative murine lymphoma mutants
25. Fusion of sequence elements from non-anchored proteins to generate a fully functional signal for glycophosphatidylinositol membrane anchor attachment
26. A nonfunctional sequence converted to a signal for glycophosphatidylinositol membrane anchor attachment
27. Requirements for glycosylphosphatidylinositol attachment are similar but not identical in mammalian cells and parasitic protozoa
28. Glycophospholipid membrane anchor attachment. Molecular analysis of the cleavage/attachment site
29. Structural and functional analysis of the Pig- A protein that is mutated in paroxysmal nocturnal hemoglobinuria
30. BiP/GRP78 but not calnexin associates with a precursor of GPI-anchored protein
31. Structure and chromosomal localization of the GPI-anchor synthesis gene PIGF and its pseudogene *PIGF
32. GAA1 recognizes the GPI anchor attachment signals and is complexed with GPI8 to form a GPI transamidase
33. Gaalp and Gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins
34. An efficient mRNA-dependent translation system from reticulocyte lysates
35. COOH-terminal processing of nascent polypeptides by the glycosylphosphatidylinositol transamidase in the presence of hydrazine is governed by the same parameters as glycosylphosphatidylinositol addition
36. Synthesis of the G.P.I. anchor
37. Regulation of site-specific N-linked glycosylation
38. N-linked glycosylation of rabies virus glycoprotein. Individual sequons differ in their glycosylation efficiencies and influence on cell surface expression
39. Efficiency of N-linked core glycosylation at asparagine-319 of rabies virus glycoprotein is altered by deletions C-terminal to the glycosylation sequon
40. Biosynthesis of glycosylphosphatidylinositol membrane anchors
41. Biosynthesis of glycosylphosphatidylinositols in mammals and unicellular microbes
42. Antigen-presenting cell engineering. The molecular toolbox
43. Prediction of omega site in nascent precursor of glycosylphosphatidylinositol protein
44. Soluble constituents of the ER lumen are required for GPI anchoring of a model protein
45. Structural and functional analysis of human germ cell alkaline phosphatase by site-specific mutagenesis
46. The affected gene underlying the class K surface protein defects. Codes for the GPI-transamidase