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Gene Review

BET1  -  Bet1p

Saccharomyces cerevisiae S288c

Synonyms: Protein SLY12, Protein transport protein BET1, SLY12, Suppressor of loss of YPT1 protein 12, YIA4C, ...
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Disease relevance of BET1

  • Temperature-sensitive mutations in BET1 caused aberrations in cell wall structure, including excretion of alpha-agglutinin into the medium, sensitivity to lysis with Zymolyase and hypersensitivity to Calcofluor White [1].

High impact information on BET1

  • The B site binds to Lxx-L/M-E sequences present in both the Bet1 and Sed5 molecules, as well as to the DxE cargo-sorting signal [2].
  • We identified a site on Sec24p that recognizes the v-SNARE Bet1p and show that packaging of a number of cargo molecules is disrupted when mutations are introduced at this site [3].
  • These vesicles contain Bos1p, Sec22p, and Ypt1p, but not Bet1p [4].
  • Furthermore, unlike Sec24p, Lst1p fails to bind to Bet1p in vitro, indicating a direct correlation between cargo binding and recruitment into vesicles [5].
  • Vesicles bearing mutations in Bet1p or Bos1p inhibit fusion with wild-type acceptor membranes, but acceptor membranes containing these mutations are fully functional [6].

Biological context of BET1


Anatomical context of BET1

  • BOS1 and BET1 are required for transport from the ER to the Golgi complex in yeast and genetically interact with each other and a subset of the other genes, whose products function at this stage of the secretory pathway [12].
  • Bos1p co-purifies with the ER to Golgi transport vesicles and co-fractionates with Bet1p and the ER membrane [12].
  • We previously identified BET3 by its genetic interactions with BET1, a gene whose SNARE-like product acts in endoplasmic reticulum (ER)-to-Golgi transport [13].
  • Among mutants that were temperature-sensitive for growth and for ability to cross-link the mannoprotein alpha-agglutinin to the cell wall, one strain was complemented by BET1, which encodes an ER-Golgi v-SNARE [1].
  • SLY2 and SLY12 encode proteins with hydrophobic tails similar to synaptobrevins, integral membrane proteins of synaptic vesicles in higher eucaryotes [10].

Associations of BET1 with chemical compounds

  • Expression of SNARE cysteine derivatives in the same strain produced a cross-linked heterodimer of Bet1p and Sec22p under oxidizing conditions [14].
  • In wild-type parental or bet1 cells, secretion of alpha-agglutinin also continued after protein synthesis was blocked with cycloheximide [1].

Regulatory relationships of BET1


Other interactions of BET1

  • Thus, this set of SNARE proteins is symmetrically distributed between vesicle and acceptor compartments, but they function asymmetrically such that Bet1p and Bos1p are required on vesicles and Sed5p activity is required on acceptor membranes [6].
  • Deletion of ISS1 had no significant effect on growth or secretion; however, iss1Delta mutants were found to be synthetically lethal with mutations in the v-SNARE genes SEC22 and BET1 [16].
  • Overexpression of SLY12 compensates for the loss of function of the ras-like GTP-binding protein Ypt1 [12].
  • Overexpression of two of them, BET1p and Sec22p, can also suppress the lethality of delta uso1, indicating that the SNAREs function downstream of Uso1p [7].
  • An analysis of BET1, BET2, and BOS1. Three factors mediating ER to Golgi transport in yeast [17].

Analytical, diagnostic and therapeutic context of BET1


  1. The ER-Golgi v-SNARE Bet1p is required for cross-linking alpha-agglutinin to the cell wall in yeast. Kipnis, P., Thomas, N., Ovalle, R., Lipke, P.N. Microbiology (Reading, Engl.) (2004) [Pubmed]
  2. SNARE selectivity of the COPII coat. Mossessova, E., Bickford, L.C., Goldberg, J. Cell (2003) [Pubmed]
  3. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Miller, E.A., Beilharz, T.H., Malkus, P.N., Lee, M.C., Hamamoto, S., Orci, L., Schekman, R. Cell (2003) [Pubmed]
  4. Bos1p, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence. Lian, J.P., Ferro-Novick, S. Cell (1993) [Pubmed]
  5. Cargo selection into COPII vesicles is driven by the Sec24p subunit. Miller, E., Antonny, B., Hamamoto, S., Schekman, R. EMBO J. (2002) [Pubmed]
  6. Asymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes. Cao, X., Barlowe, C. J. Cell Biol. (2000) [Pubmed]
  7. Assembly of the ER to Golgi SNARE complex requires Uso1p. Sapperstein, S.K., Lupashin, V.V., Schmitt, H.D., Waters, M.G. J. Cell Biol. (1996) [Pubmed]
  8. BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex. Newman, A.P., Shim, J., Ferro-Novick, S. Mol. Cell. Biol. (1990) [Pubmed]
  9. Characterization of new mutants in the early part of the yeast secretory pathway isolated by a [3H]mannose suicide selection. Newman, A.P., Ferro-Novick, S. J. Cell Biol. (1987) [Pubmed]
  10. Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily. Dascher, C., Ossig, R., Gallwitz, D., Schmitt, H.D. Mol. Cell. Biol. (1991) [Pubmed]
  11. Nucleotide sequence and analysis of the centromeric region of yeast chromosome IX. Voss, H., Tamames, J., Teodoru, C., Valencia, A., Sensen, C., Wiemann, S., Schwager, C., Zimmermann, J., Sander, C., Ansorge, W. Yeast (1995) [Pubmed]
  12. Bos1p, a membrane protein required for ER to Golgi transport in yeast, co-purifies with the carrier vesicles and with Bet1p and the ER membrane. Newman, A.P., Groesch, M.E., Ferro-Novick, S. EMBO J. (1992) [Pubmed]
  13. TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion. Sacher, M., Jiang, Y., Barrowman, J., Scarpa, A., Burston, J., Zhang, L., Schieltz, D., Yates, J.R., Abeliovich, H., Ferro-Novick, S. EMBO J. (1998) [Pubmed]
  14. Cysteine-disulfide cross-linking to monitor SNARE complex assembly during endoplasmic reticulum-Golgi transport. Flanagan, J.J., Barlowe, C. J. Biol. Chem. (2006) [Pubmed]
  15. Bet1p activates the v-SNARE Bos1p. Stone, S., Sacher, M., Mao, Y., Carr, C., Lyons, P., Quinn, A.M., Ferro-Novick, S. Mol. Biol. Cell (1997) [Pubmed]
  16. Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae. Kurihara, T., Hamamoto, S., Gimeno, R.E., Kaiser, C.A., Schekman, R., Yoshihisa, T. Mol. Biol. Cell (2000) [Pubmed]
  17. An analysis of BET1, BET2, and BOS1. Three factors mediating ER to Golgi transport in yeast. Ferro-Novick, S., Newman, A.P., Groesch, M., Ruohola, H., Rossi, G., Graf, J., Shim, J. Cell Biophys. (1991) [Pubmed]
  18. Yeast ER-Golgi v-SNAREs Bos1p and Bet1p differ in steady-state localization and targeting. Ossipov, D., Schröder-Köhne, S., Schmitt, H.D. J. Cell. Sci. (1999) [Pubmed]
  19. Characteristics of endoplasmic reticulum-derived transport vesicles. Rexach, M.F., Latterich, M., Schekman, R.W. J. Cell Biol. (1994) [Pubmed]
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