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

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Gene Review: 

GAB1  -  Gab1p

Saccharomyces cerevisiae S288c

Synonyms: CDC91, Cell division control protein 91, GPI transamidase component GAB1, L9122.2, YLR459W
 
 
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High impact information on GAB1

  • From these data, we derived a consensus sequence which predicts high-affinity binding to PtdIns(3, 4)P2 and/or PtdIns(3,4,5)P3, and we have identified several new PH domain-containing proteins that bind PI3K products, including Gab1, Dos, myosinX, and Sbf1 [1].
  • The essential GAB1 gene, which encodes an endoplasmic reticulum (ER)-membrane protein, was identified in a screen for mutants defective in cellular morphogenesis [2].
  • Deficiencies in the endoplasmic reticulum (ER)-membrane protein Gab1p perturb transfer of glycosylphosphatidylinositol to proteins and cause perinuclear ER-associated actin bar formation [2].
  • These findings suggest that Gab1p is a subunit of the GPI transamidase with distinct relationships to other subunits in the same complex [2].
  • In addition, both Gab1p and Gpi17p localize to the ER and are in the same protein complex in vivo [2].

References

  1. Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast. Isakoff, S.J., Cardozo, T., Andreev, J., Li, Z., Ferguson, K.M., Abagyan, R., Lemmon, M.A., Aronheim, A., Skolnik, E.Y. EMBO J. (1998) [Pubmed]
  2. 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]
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