The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

WBP1  -  Wbp1p

Saccharomyces cerevisiae S288c

Synonyms: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1, Oligosaccharyl transferase subunit WBP1, Oligosaccharyl transferase subunit beta, YEL002C
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on WBP1

  • The beta and delta subunits of the oligosaccharyltransferase are encoded by the WBP1 and SWP1 genes [1].
  • The Saccharomyces cerevisiae oligosaccharyltransferase was purified as a heteroligomeric complex consisting of six subunits (alpha-zeta) having apparent molecular masses of 64 kD (Ost1p), 45 kD (Wbp1p), 34 kD, 30 kD (Swp1p), 16 kD, and 9 kD [2].
  • To analyze the role of this motif in yeast, we constructed a SUC2-WBP1 chimera consisting of the coding sequence for the normally secreted glycoprotein invertase fused to the coding sequence of the COOH terminus (including the transmembrane domain and 16-amino acid cytoplasmic tail) of Wbplp [3].
  • Subcellular fractionation revealed that > 90% of the alpha 1,6 mannose-modified fusion protein colocalized with the ER (Wbp1p) and not with the Golgi Och1p-containing compartment or other membrane fractions [3].
  • The Saccharomyces cerevisiae Wbp1 protein is an endoplasmic reticulum (ER), type I transmembrane protein which contains a cytoplasmic dilysine (KKXX) motif [3].

Biological context of WBP1


Anatomical context of WBP1

  • In addition, in vitro N-glycosylation of the acceptor peptide Tyr-Asn-Leu-Thr-Ser-Val using microsomal membranes from WBP1 depleted cells is reduced as compared with membranes from wild-type cells [7].
  • In contrast to results with alpha-COP mutants, we found that Emp47p was mislocalised to the vacuole in mutants affecting beta'-, gamma-, delta-, and zeta-COP subunits of coatomer and that the mutant coatomer bound neither to the Emp47p nor to the Wbp1p di-lysine signal in vitro [8].

Associations of WBP1 with chemical compounds

  • Carbohydrate analysis of the invertase-Wbp1 fusion protein using mannose linkage-specific antiserum demonstrated that the fusion protein was efficiently modified by the early Golgi initial alpha 1,6 mannosyltransferase (Och1p) [3].
  • An octapeptide corresponding to the C-terminal tail of Wbp1p, a component of the yeast N-oligosaccharyltransferase complex, has been synthesized with a photoreactive phenylalanine at position -5 and was radioactively labeled with [125I]iodine at a tyrosine residue introduced at the N terminus of the peptide [9].

Physical interactions of WBP1

  • The OT subunit Wbp1p was found to interact very strongly with Sec61p and Sbh1p and weakly with Sss1p [10].

Other interactions of WBP1

  • Depletion of WBP1 correlates with a defect in transferring core oligosaccharides to carboxypeptidase Y and proteinase A in vivo [7].
  • Reporter molecules were constructed by replacing parts of a control invertase-Wbp1p chimera with those of Emp24p, and their transport rates were assessed [11].

Analytical, diagnostic and therapeutic context of WBP1


  1. The alpha subunit of the Saccharomyces cerevisiae oligosaccharyltransferase complex is essential for vegetative growth of yeast and is homologous to mammalian ribophorin I. Silberstein, S., Collins, P.G., Kelleher, D.J., Rapiejko, P.J., Gilmore, R. J. Cell Biol. (1995) [Pubmed]
  2. Functional characterization of Ost3p. Loss of the 34-kD subunit of the Saccharomyces cerevisiae oligosaccharyltransferase results in biased underglycosylation of acceptor substrates. Karaoglu, D., Kelleher, D.J., Gilmore, R. J. Cell Biol. (1995) [Pubmed]
  3. Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast. Gaynor, E.C., te Heesen, S., Graham, T.R., Aebi, M., Emr, S.D. J. Cell Biol. (1994) [Pubmed]
  4. New findings on interactions among the yeast oligosaccharyl transferase subunits using a chemical cross-linker. Yan, A., Ahmed, E., Yan, Q., Lennarz, W.J. J. Biol. Chem. (2003) [Pubmed]
  5. The genetic interaction of kar2 and wbp1 mutations. Distinct functions of binding protein BiP and N-linked glycosylation in the processing pathway of secreted proteins in Saccharomyces cerevisiae. te Heesen, S., Aebi, M. Eur. J. Biochem. (1994) [Pubmed]
  6. The N-oligosaccharyltransferase complex from yeast. Knauer, R., Lehle, L. FEBS Lett. (1994) [Pubmed]
  7. The yeast WBP1 is essential for oligosaccharyl transferase activity in vivo and in vitro. te Heesen, S., Janetzky, B., Lehle, L., Aebi, M. EMBO J. (1992) [Pubmed]
  8. Alpha-COP can discriminate between distinct, functional di-lysine signals in vitro and regulates access into retrograde transport. Schröder-Köhne, S., Letourneur, F., Riezman, H. J. Cell. Sci. (1998) [Pubmed]
  9. Nonclathrin coat protein gamma, a subunit of coatomer, binds to the cytoplasmic dilysine motif of membrane proteins of the early secretory pathway. Harter, C., Pavel, J., Coccia, F., Draken, E., Wegehingel, S., Tschochner, H., Wieland, F. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  10. Subunits of the translocon interact with components of the oligosaccharyl transferase complex. Chavan, M., Yan, A., Lennarz, W.J. J. Biol. Chem. (2005) [Pubmed]
  11. Identification of potential regulatory elements for the transport of Emp24p. Nakamura, N., Yamazaki, S., Sato, K., Nakano, A., Sakaguchi, M., Mihara, K. Mol. Biol. Cell (1998) [Pubmed]
  12. A specific segment of the transmembrane domain of Wbp1p is essential for its incorporation into the oligosaccharyl transferase complex. Li, G., Yan, Q., Oen, H.O., Lennarz, W.J. Biochemistry (2003) [Pubmed]
WikiGenes - Universities