Oligosaccharyl transferase: Gatekeeper to the secretory pathway

Current Opinion in Chemical Biology

Volumn 6, Issue 6, 2002, Pages 844-850

  Dempski Jr , Robert E ^a   Imperiali, Barbara ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE LINKED OLIGOSACCHARIDE; ENZYME; OLIGOSACCHARIDE; PROTEIN; TRANSFERASE; DOLICHYL DIPHOSPHOOLIGOSACCHARIDE PROTEIN GLYCOTRANSFERASE; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE - PROTEIN GLYCOTRANSFERASE; GLYCOPROTEIN; GLYCOSYLTRANSFERASE; MEMBRANE PROTEIN;

BIOSYNTHESIS; CONSERVATION BIOLOGY; ENDOPLASMIC RETICULUM; NONHUMAN; PROTEIN ANALYSIS; REVIEW; SECRETION; AMINO ACID SEQUENCE; ANIMAL; CARBOHYDRATE ANALYSIS; CHEMISTRY; DISORDERS OF CARBOHYDRATE METABOLISM; ENZYMOLOGY; GENETICS; GLYCOSYLATION; GOLGI COMPLEX; HUMAN; METABOLISM; MOLECULAR GENETICS; MUTATION; PROTEIN PROCESSING; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY;

PYRONIA TITHONUS;

AMINO ACID SEQUENCE; ANIMALS; CARBOHYDRATE METABOLISM, INBORN ERRORS; CARBOHYDRATE SEQUENCE; ENDOPLASMIC RETICULUM; GLYCOPROTEINS; GLYCOSYLATION; GOLGI APPARATUS; HEXOSYLTRANSFERASES; HUMANS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID; TRANSFERASES;

EID: 0036899975     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(02)00390-3     Document Type: Review

References (53)

1. Gavel Y., von Heijne G. Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng. 3:1990;433-442.
2. Mononen I., Karjalainen E. Structural comparison of protein sequences around potential N-glycosylation sites. Biochim Biophys Acta. 788:1999;364-367.
3. Johnson A., van Waes M. The translocon: a dynamic gateway at the ER membrane. Annu Rev Cell Dev Biol. 19:1999;87-119.
4. Young B., Craven R., Reid P., Willer M., Stirling C. Sec63p and Far2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo. EMBO J. 20:2001;262-271. The authors have identified essential proteins involved in translocating the nascent polypeptide into the ER.
5. Potter M., Nicchitta C. Endoplasmic reticulum-bound ribosomes reside in stable association with the translocon following termination of protein synthesis. J Biol Chem. 277:2002;23314-23320. The authors have determined that the ribosome remains bound to the ER membrane and translocation machinery until a protein that lacks a signal sequence is being synthesized.
6. Van Valkenburgh C., Chen X., Mullins C., Fang H., Green N. The catalytic mechanism of endoplasmic reticulum signal peptidase appears to be distinct from most eubacterial signal peptidases. J Biol Chem. 274:1999;11519-11525.
7. Nilsson I., von Heijne G. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J Biol Chem. 268:1993;5798-5801.
8. Chen X., Van Valkenburgh C., Liang H., Fang H., Green N. Signal peptidase and oligosaccharyltransferase interact in a sequential and dependent manner within the endoplamic reticulum. J Biol Chem. 276:2001;2411-2416.
9. Ellgaard L., Helenius A. ER quality control: towards an understanding at the molecular level. Curr Opin Cell Biol. 13:2001;431-437.
10. Burda P., Aebi M. The dolichol pathway of N-linked glycosylation. Biochim Biophys Acta. 1426:1999;239-257.
11. 5 across the ER membrane into the lumen.
12. Kelleher D., Karaoglu D., Gilmore R. Large-scale isolation of dolichol-linked oligosaccharides with homogeneous oligosaccharide structures: determination of steady-state dolichol-linked oligosaccharide compositions. Glycobiology. 11:2001;321-333.
13. Kararoglu D., Kelleher D., Gilmore R. Allosteric regulation provides a molecular mechanism for preferential utilization of the fully assembled dolichol-linked oligosaccharide by the yeast oligosaccharyl transferase. Biochemistry. 40:2001;12193-12206. The authors have examined the relative turnover rate for several oligosaccharide substrates and have proposed two binding sites for the oligosaccharide substrate.
14. Duvet S., Chirat F., Mit A., Verbert A., Dubuisson J., Cacan R. Reciprocal relationship between α-1,2 mannosidase processing and reglucosylation in the rough endoplasmic reticulum of Man-P-Dol deficient cells. Eur J Biochem. 267:2000;1146-1152.
15. Foulquier F., Harduin-Lepers A., Duvet S., Marchal I., Mir A., Delannoy P., Chirat F., Cacan R. The unfolded protein response in a dolichyl phosphate mannose-deficient Chinese hamster ovary cell line points out the key role of a demannosylation step in the quality-control mechanism of N-glycoproteins. Biochem J. 362:2002;491-498.
16. Bosch M., Trometta S., Engstrom U., Parodi A. Characterization of dolichol diphosphate oligosaccharide: protein oligosaccharyltransferase and glycoprotein-processing glucosidases occurring in trypanosomatid protozoa. J Biol Chem. 263:1988;17360-17365.
17. Parodi A. N-Glycosylation in trypanosomatid protozoa. Glycobiology. 3:1993;193-199.
18. 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;285-304.
19. Pathak R., Parker C., Imperiali B. The essential NLT1 gene encodes the 64 kDa glycoprotein subunit of the oligosaccharyl transferase. FEBS Lett. 362:1995;229-234.
20. Knauer R., Lehle L. The N-oligosaccharyltransferase complex from yeast. FEBS Lett. 344:1994;83-86.
21. Pathak R., Imperiali B. A dual affinity tag on the 64-kDa Nlt1p subunit allows the rapid characterization of mutant yeast oligosaccharyl transferase complexes. Arch Biochem Biophys. 338:1997;1-6.
22. Kelleher D., Gilmore R. The Saccharomyces cerevisiae oligosaccharyltransferase is a protein complex composed of Wbp1p, Swp1p, and 4 additional polypeptides. J Biol Chem. 269:1994;12908-12917.
23. Knauer R., Lehle L. The oligosaccharyltransferase complex from Saccharomyces cerevisiae: isolation of the Ost6p gene, its synthetic interaction with Ost3p, and analysis of the native complex. J Biol Chem. 274:1999;17249-17256.
24. Karaoglu D., Kelleher D., Gilmore R. The highly conserved Stt3p protein is a subunit of the yeast oligosaccharyl transferase and forms a subcomplex with Ost3p and Ost4p. J Biol Chem. 272:1997;32513-32520.
25. Spirig U., Glaras M., Bodmer D., Reiss G., Burda P., Lippuner V., te Hessen S., Aebi M. The Stt3 protein is a component of the yeast oligosaccharyltransferase complex. Mol Gen Genet. 256:1997;628-637.
26. Silberstein S., Collins P., Kelleher D., Gilmore R. The essential Ost2 gene encodes the 16-KD subunit of the yeast oligosaccharyltransferase, a highly conserved protein expressed in diverse eukaryotic organisms. J Cell Biol. 131:1995;371-383.
27. Zufferey R., Knauer R., Burda P., Stagljar I., te Hessen S., Lehle L., Aebi M. Stt3p, a highly conserved protein required for yeast oligosaccharyltransferase activity in vivo. EMBO J. 14:1995;4949-4960.
28. te Hessen S., Knauer R., Lehle L., Aebi M. Yeast Wbp1p and Swp1p form a protein complex essential for oligosaccharyltransferase activity. EMBO J. 12:1993;279-284.
29. Yan Q., Lennarz W. Oligosaccharyltransferase: a complex multisubunit enzyme of the endoplasmic reticulum. Biochem Biophys Res Commun. 266:1999;684-689.
30. Park H., Lennarz W. Evidence for interaction of yeast protein kinase C with several subunits of oligosaccharyltransferase. Glycobiology. 10:2000;737-744.
31. Stagljar I., Korostensky C., Johnsson N., te Hessen S. A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proc Natl Acad Sci USA. 95:1998;5187-5192.
32. te Hessen S., Rauhut R., Aebersold R., Abelson J., Aebi M., Clark M. An essential 45 kDa yeast transmembrane protein reacts with anti-nuclear pore antibodies: purification of the protein, immunolocalization and cloning of the gene. Eur J Cell Biol. 56:1991;8-18.
33. Knauer R., Lehle L. The oligosaccharyltransferase complex from yeast. Biochim Biophys Acta. 1426:1999;259-273.
34. Makishima T., Nakashima T., Nagata-Kuno K., Fukushima K., Iida H., Sakaguchi M., Ikehara Y., Komiyama S., Nishimoto T. The highly conserved DAD1 protein involved in apoptosis is required for N-linked glycosylation. Genes Cells. 2:1997;129-141.
35. Silberstein S., Collins P., Kelleher D., Rapiejko P., Gilmore R. The α subunit of the Saccharomyces cerevisiae oligosaccharyltransferase complex is essential for vegetative growth of yeast and is homologous to mammalian ribophorin I. J Cell Biol. 128:1995;525-536.
36. Yan Q., Prestwich G., Lennarz W. The Ost1p subunit of yeast oligosaccharyltransferase recognizes the peptide glycosylation site sequence, -Asn-X-Ser-Thr. J Biol Chem. 274:1999;5021-5025. The authors have developed a photo-affinity peptide substrate to probe the binding site of the OT.
37. Reiss G., te Hessen S., Gilmore R., Zufferey R., Aebi M. A specific screen for oligosaccharyltransferase mutations identifies the 9 kDa OST5 protein required for optimal activity in vivo and in vitro. EMBO J. 16:1997;1164-1172.
38. Yoshida S., Ohya Y., Nakano A., Anraku Y. STT3, a novel essential gene related to the PKC1/STT1 protein kinase pathway, is involved in protein glycosylation in yeast. Gene. 164:1995;167-172.
39. Wacker M, Nita-Lazar M, Aebi M: PglB, an oligosaccharyltransferase in the eubacterium Campylobacter jejuni? Glycobiology 2001, 11.
40. Gutiérrez A., Sánchez-López R., Ramos M., Alagón A. Cloning of the entamoeba histolytica STT3 gene, a subunit of the oligosaccharyltransferase complex. Arch Med Res. 31:2000;S162-S164.
41. Young N., Brisson J., Kelly J., Watson D., Tessier L., Lanthier P., Jarrell H., Cadotte N., St. Michael F., Aberg E., et al. Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni. J Biol Chem. 277:2002;42530-42539. The first data showing the presence of N-linked glycosylation in Gram-negative bacteria.
42. Karaoglu D., Kelleher D., Gilmore R. Functional characterization of Ost3p. Loss of the 34-kD subunit of the Saccharomyces cerevisiae oligosaccharyltransferase results in biased underglycosylation of acceptor substrates. J Cell Biol. 130:1995;567-577.
43. Kim H., Park H., Montalvo L., Lennarz W. Studies on the role of the hydrophobic domain of Ost4p in interactions with other subunits of yeast oligosaccharyltransferase. Proc Natl Acad Sci USA. 97:2000;1516-1520.
44. Marek K., Vijay I., Marth J. A recessive deletion in the GlcNAc-1-phosphotransferase gene results in periimplantation embryonic lethality. Glycobiology. 9:1999;1263-1271.
45. Matthijs G., Jaeken J. Congenital disorders of glycosylation. Annu Rev Genom Hum Genet. 2:2001;129-151. A comprehensive review of CDGs, including genotypic and phenotypic data.
46. Burda P., Jakob C., Beinhauer J., Hegemann J., Aebi M. Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases. Glycobiology. 9:1999;617-625.
47. 2-PP-dolichyl mannosyltransferase. J Biol Chem. 277:2002;25815-25822.
48. Matthijs G., Schollen E., Pardon E., Veiga Da Cunha M., Jaeken J., Cassiman J., van Schaftingen E. Mutations in PMM2, a phosphomannomutase gene on chromosome 16p13, in carbohydrate-deficient glycoprotein type 1 syndrome (Jaeken syndrome). Nat Genet. 16:1997;88-92.
49. Matthijs G., Schollen E., Van Schaftingen E., Cassiman J., Jaeken J. Lack of homozygotes for the most frequent disease allele in carbohydrate-deficient glycoprotein syndrome type 1A. Am J Hum Genet. 62:1998;542-550.
50. Tayebi N., Andrews D., Park J., Orvisky E., McReynolds J., Sidransky E., Krasnewich D. A deletion-insertion mutation in the phosphomannomutase 2 gene in an African American patient with congenital disorders of glycosylation-Ia. Am J Med Genet. 108:2002;241-246.
51. Matthijs G., Schollen E., Bjursell C., Erlanden A., Freeze H., Imtiaz F., Kjaergaard S., Martinsson T., Schwartz M., Seta N., et al. Mutations in PMM2 that cause congenital disorders of glycosylation, type Ia (CDG-Ia). Hum Mutat. 16:2000;386-394. A summary of point mutations that result in CDG-Ia. This paper includes a website with updated data on new patients diagnosed with this disease.Now In PressThe work referred to in the text as (M Aebi, personal communication) is now in press.
52. Wackler M, Linton D, Hitchen PG, Nita-Lazar M, Haslam SM, North SJ, Panico M, Morris HR, Dell A, Wren BW, Aebi M: N-linked protein glycosylation in Campylobacter jejuni and its functional transfer into Escherichia coli. Science 2002, in press. The authors identify the glycosylation machinery from a bacterium, C. jejuni, as well as transfering the functional glycosylation machinery to E. coli. Now In Press The work referred to in the text as (M Aebi, personal communication) is now in press.
53. Yan Q, Lennarz WJ: Studies on the function of oligosaccharyl transferase subunits: Stt3p is directly involved in the glycosylation process. J Biol Chem 2002, in press. Recently, Lennarz and co-workers have presented evidence that indicates that the Stt3p subunit may be the primary binding site for glycosylatable peptides in OT.