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Gene Review

TLG2  -  Tlg2p

Saccharomyces cerevisiae S288c

Synonyms: Syntaxin TLG2, T-SNARE affecting a late Golgi compartment protein 2, YOL018C
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High impact information on TLG2

  • The SM protein Vps45p binds its Sx Tlg2p in a manner analogous to that captured by the Sly1p-Sed5p crystal structure, whereby the NH2-terminal peptide of the Sx inserts into a hydrophobic pocket on the outer face of domain I of the SM protein [1].
  • Studies of the yeast trans-Golgi network (TGN)/endosomal SNARE complex, which includes the syntaxin-like SNARE Tlg2p, have suggested that its assembly requires activation by binding of the SM protein Vps45p to the cytoplasmic region of Tlg2p folded into a closed conformation [2].
  • The t-SNARE in a late Golgi compartment (Tlg2p) syntaxin is required for endocytosis and localization of cycling proteins to the late Golgi compartment in yeast [3].
  • Fractionation and protease protection experiments indicate that Tlg2p is required prior to or at the step of API segregation into the Cvt vesicle [4].
  • We describe here the remaining two, Tlg1p and Tlg2p [5].

Biological context of TLG2

  • TLG2 is not an essential gene, and its deletion does not cause defects in the secretory pathway [6].
  • Since a deltavps45 deltatlg2 double mutant has a more severe vacuolar protein sorting defect than a deltatlg2 mutant, Vps45p cannot only interact with Tlg2p [7].
  • These results strongly suggest that Tlg2p is a t-SNARE involved in early endosome biogenesis [6].
  • Finally, we found that mutation of single PKA sites in Tlg1 (Ser31 to Ala31) or Tlg2 (Ser90 to Ala90) was sufficient to restore endocytosis, but not exocytosis, to snc cells [8].

Anatomical context of TLG2


Other interactions of TLG2

  • Notably, Snc1(ala43) was found to be nonfunctional in cells lacking Tlg1 or Tlg2 [11].
  • The Sec1p homologue Vps45p binds to the syntaxin Tlg2p [7].
  • Thus, the early Vps45-Tlg2p-dependent step of the Cvt pathway appears to be mechanistically distinct from the comparable stage in macroautophagy [4].
  • However, its deletion in cells lacking the vacuolar ATPase subunit Vma2p leads to loss of viability, suggesting that Tlg2p is involved in endocytosis [6].
  • However, Snc2p binds in vivo to many other syntaxin-like t-SNAREs, and binding of Sncp to the endosomal/Golgi t-SNARE Tlg2p is also reduced in sec4-8 cells [12].


  1. The Sec1p/Munc18 protein Vps45p binds its cognate SNARE proteins via two distinct modes. Carpp, L.N., Ciufo, L.F., Shanks, S.G., Boyd, A., Bryant, N.J. J. Cell Biol. (2006) [Pubmed]
  2. How Tlg2p/syntaxin 16 'snares' Vps45. Dulubova, I., Yamaguchi, T., Gao, Y., Min, S.W., Huryeva, I., Südhof, T.C., Rizo, J. EMBO J. (2002) [Pubmed]
  3. A t-SNARE of the endocytic pathway must be activated for fusion. Paumet, F., Brügger, B., Parlati, F., McNew, J.A., Söllner, T.H., Rothman, J.E. J. Cell Biol. (2001) [Pubmed]
  4. Cytoplasm to vacuole trafficking of aminopeptidase I requires a t-SNARE-Sec1p complex composed of Tlg2p and Vps45p. Abeliovich, H., Darsow, T., Emr, S.D. EMBO J. (1999) [Pubmed]
  5. Two syntaxin homologues in the TGN/endosomal system of yeast. Holthuis, J.C., Nichols, B.J., Dhruvakumar, S., Pelham, H.R. EMBO J. (1998) [Pubmed]
  6. A yeast t-SNARE involved in endocytosis. Séron, K., Tieaho, V., Prescianotto-Baschong, C., Aust, T., Blondel, M.O., Guillaud, P., Devilliers, G., Rossanese, O.W., Glick, B.S., Riezman, H., Keränen, S., Haguenauer-Tsapis, R. Mol. Biol. Cell (1998) [Pubmed]
  7. The Sec1p homologue Vps45p binds to the syntaxin Tlg2p. Nichols, B.J., Holthuis, J.C., Pelham, H.R. Eur. J. Cell Biol. (1998) [Pubmed]
  8. t-SNARE phosphorylation regulates endocytosis in yeast. Gurunathan, S., Marash, M., Weinberger, A., Gerst, J.E. Mol. Biol. Cell (2002) [Pubmed]
  9. Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures. Abeliovich, H., Grote, E., Novick, P., Ferro-Novick, S. J. Biol. Chem. (1998) [Pubmed]
  10. SNAREs and membrane fusion in the Golgi apparatus. Nichols, B.J., Pelham, H.R. Biochim. Biophys. Acta (1998) [Pubmed]
  11. Yeast exocytic v-SNAREs confer endocytosis. Gurunathan, S., Chapman-Shimshoni, D., Trajkovic, S., Gerst, J.E. Mol. Biol. Cell (2000) [Pubmed]
  12. Promiscuity in Rab-SNARE interactions. Grote, E., Novick, P.J. Mol. Biol. Cell (1999) [Pubmed]
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