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Gene Review

SEC22  -  Sec22p

Saccharomyces cerevisiae S288c

Synonyms: L8479.3, Protein transport protein SEC22, SLY2, Suppressor of loss of YPT1 protein 2, TS26, ...
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High impact information on SEC22

  • By electron microscopy three of the mutants, sec18, sec17, and sec22, accumulate 50 nm vesicles at the nonpermissive temperature [1].
  • Weaker suppression is evident upon overexpression of genes encoding the vesicle-SNAREs SEC22, BET1, or YKT6 [2].
  • It forms a SNARE complex with Sec22 and the ER syntaxin Ufe1 [3].
  • Sed5 is known to combine with two light chains (Bos1 and Sec22) to form the t-SNARE needed to receive vesicles from the endoplasmic reticulum [4].
  • Sly1p-depleted cells, as well as a conditional lethal sly2 null mutant at nonpermissive temperatures, accumulate ER membranes and core-glycosylated invertase and carboxypeptidase Y [5].

Biological context of SEC22

  • We isolated mutant yeast strains in which SEC22 gene function, which in a wild type strain background is non-essential for cell viability, has become essential [6].

Anatomical context of SEC22


Regulatory relationships of SEC22

  • Moreover, overexpression of ISS1 could suppress mutations in SEC22 [10].

Other interactions of SEC22

  • 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 [10].
  • In wild-type cells Kex2p-cleavage is observed only when Sec22-alpha is greatly overproduced [11].

Analytical, diagnostic and therapeutic context of SEC22

  • Immunofluorescence microscopy and subcellular fractionation studies showed that Sec22-alpha is returned to the ER from the late Golgi (Kex2p) compartment [11].


  1. Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway. Kaiser, C.A., Schekman, R. Cell (1990) [Pubmed]
  2. Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking. VanRheenen, S.M., Cao, X., Lupashin, V.V., Barlowe, C., Waters, M.G. J. Cell Biol. (1998) [Pubmed]
  3. A SNARE required for retrograde transport to the endoplasmic reticulum. Burri, L., Varlamov, O., Doege, C.A., Hofmann, K., Beilharz, T., Rothman, J.E., Söllner, T.H., Lithgow, T. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  4. Distinct SNARE complexes mediating membrane fusion in Golgi transport based on combinatorial specificity. Parlati, F., Varlamov, O., Paz, K., McNew, J.A., Hurtado, D., Söllner, T.H., Rothman, J.E. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  5. The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport. Ossig, R., Dascher, C., Trepte, H.H., Schmitt, H.D., Gallwitz, D. Mol. Cell. Biol. (1991) [Pubmed]
  6. The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast. Andag, U., Neumann, T., Schmitt, H.D. J. Biol. Chem. (2001) [Pubmed]
  7. Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes. Legesse-Miller, A., Sagiv, Y., Glozman, R., Elazar, Z. J. Biol. Chem. (2000) [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. 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]
  10. 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]
  11. Recycling of the yeast v-SNARE Sec22p involves COPI-proteins and the ER transmembrane proteins Ufe1p and Sec20p. Ballensiefen, W., Ossipov, D., Schmitt, H.D. J. Cell. Sci. (1998) [Pubmed]
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