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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

GPI17  -  Gpi17p

Saccharomyces cerevisiae S288c

Synonyms: D9461.20, GPI transamidase component GPI17, YDR434W
 
 
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High impact information on GPI17

  • In addition, both Gab1p and Gpi17p localize to the ER and are in the same protein complex in vivo [1].
  • The transamidation depends on a complex of four proteins, Gaa1p, Gpi8p, Gpi16p and Gpi17p [2].
 

Other interactions of GPI17

  • Moreover, Gpi8p becomes unstable when any one of the other subunits is depleted, whereas Gpi17p is slightly affected only by the depletion of Gaa1p [3].
 

Analytical, diagnostic and therapeutic context of GPI17

  • Random and site-directed mutagenesis generated mutations in several highly conserved amino acids but did not yield nonfunctional alleles of Gpi17p and a saturating screen did not yield any dominant negative alleles of Gpi17p [3].

References

  1. Deficiencies in the endoplasmic reticulum (ER)-membrane protein Gab1p perturb transfer of glycosylphosphatidylinositol to proteins and cause perinuclear ER-associated actin bar formation. Grimme, S.J., Gao, X.D., Martin, P.S., Tu, K., Tcheperegine, S.E., Corrado, K., Farewell, A.E., Orlean, P., Bi, E. Mol. Biol. Cell (2004) [Pubmed]
  2. The glycosylphosphatidylinositol (GPI) signal sequence of human placental alkaline phosphatase is not recognized by human Gpi8p in the context of the yeast GPI anchoring machinery. Meyer, U., Fraering, P., Bosson, R., Imhof, I., Benghezal, M., Vionnet, C., Conzelmann, A. Mol. Microbiol. (2002) [Pubmed]
  3. Gpi17p does not stably interact with other subunits of glycosylphosphatidylinositol transamidase in Saccharomyces cerevisiae. Zhu, Y., Fraering, P., Vionnet, C., Conzelmann, A. Biochim. Biophys. Acta (2005) [Pubmed]
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