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GCS1  -  Gcs1p

Saccharomyces cerevisiae S288c

Synonyms: ADP-ribosylation factor GTPase-activating protein GCS1, ARF GAP GCS1, YDL226C
 
 
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High impact information on GCS1

  • Our results demonstrate that the Gcs1 + Age2 ArfGAP pair provides overlapping function for transport from the TGN, and also indicate that multiple activities at the TGN can be maintained with the aid of a single ArfGAP [1].
  • Further, we demonstrate novel direct interactions of coatomer subunits with regulatory proteins: beta'- and gamma-COP interact with the ARF-GTP-activating protein (GAP) Glo3p, but not Gcs1p, and beta- and epsilon-COP interact with ARF-GTP [2].
  • The cloning and molecular characterization of the GCS1 gene from the budding yeast Saccharomyces cerevisiae show that stationary phase is in fact a unique developmental state, with requirements to resume cell proliferation that can be distinct from those for maintenance of proliferation [3].
  • A point mutation within the finger motif produces a phenotype that mimics that of deletion of the GCS1 gene, showing that the finger motif is essential for full Gcs1p activity [3].
  • The budding yeast Saccharomyces cerevisiae contains a family of Arf (ADP-ribosylation factor) GTPase activating protein (GAP) proteins with the Gcs1 + Age2 ArfGAP pair providing essential overlapping function for the movement of transport vesicles from the trans-Golgi network [4].
 

Biological context of GCS1

 

Anatomical context of GCS1

  • Synthetic lethality was observed between null alleles of GCS1 and SLA2, the gene encoding a protein involved in stabilization of the actin cytoskeleton [6].
  • Furthermore, Gcs1 function is needed for the efficient secretion of invertase, as expected for a component of vesicle transport [8].
  • The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function for transport from the yeast trans-Golgi network [1].
  • Genetic and in vitro approaches reveal that Glo3 and Gcs1 have an overlapping essential function at the endoplasmic reticulum (ER)-Golgi stage of vesicular transport [9].
  • In gcs1 mutant cells, the fraction of Arl1p in cytosol relative to trans-Golgi was less than it was in wild-type cells [10].
 

Associations of GCS1 with chemical compounds

 

Physical interactions of GCS1

 

Regulatory relationships of GCS1

  • Taken together, these results indicate that GCS1 is essential for sporulation and suggest that GCS1 positively regulates SPO14 [11].
 

Other interactions of GCS1

  • Prenylated isoforms of yeast casein kinase I, including the novel Yck3p, suppress the gcs1 blockage of cell proliferation from stationary phase [5].
  • In addition, synthetic growth defects were observed between null alleles of GCS1 and SAC6, the gene encoding the yeast fimbrin homologue [6].
  • Saccharomyces cerevisiae Gcs1 is an ADP-ribosylation factor GTPase-activating protein [8].
  • Only gcs1delta mutants display a sporulation defect similar to that of spo14 mutants: cells deleted for GCS1 initiate the sporulation program but are defective in synthesis of the prospore membrane [11].
  • Role for Gcs1p in regulation of Arl1p at trans-Golgi compartments [10].

References

  1. The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function for transport from the yeast trans-Golgi network. Poon, P.P., Nothwehr, S.F., Singer, R.A., Johnston, G.C. J. Cell Biol. (2001) [Pubmed]
  2. COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP. Eugster, A., Frigerio, G., Dale, M., Duden, R. EMBO J. (2000) [Pubmed]
  3. A member of a novel family of yeast 'zn-finger' proteins mediates the transition from stationary phase to cell proliferation. Ireland, L.S., Johnston, G.C., Drebot, M.A., Dhillon, N., DeMaggio, A.J., Hoekstra, M.F., Singer, R.A. EMBO J. (1994) [Pubmed]
  4. Membrane metabolism mediated by Sec14 family members influences Arf GTPase activating protein activity for transport from the trans-Golgi. Wong, T.A., Fairn, G.D., Poon, P.P., Shmulevitz, M., McMaster, C.R., Singer, R.A., Johnston, G.C. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  5. Prenylated isoforms of yeast casein kinase I, including the novel Yck3p, suppress the gcs1 blockage of cell proliferation from stationary phase. Wang, X., Hoekstra, M.F., DeMaggio, A.J., Dhillon, N., Vancura, A., Kuret, J., Johnston, G.C., Singer, R.A. Mol. Cell. Biol. (1996) [Pubmed]
  6. GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro. Blader, I.J., Cope, M.J., Jackson, T.R., Profit, A.A., Greenwood, A.F., Drubin, D.G., Prestwich, G.D., Theibert, A.B. Mol. Biol. Cell (1999) [Pubmed]
  7. The functional relationship between the Cdc50p-Drs2p putative aminophospholipid translocase and the Arf GAP Gcs1p in vesicle formation in the retrieval pathway from yeast early endosomes to the TGN. Sakane, H., Yamamoto, T., Tanaka, K. Cell Struct. Funct. (2006) [Pubmed]
  8. Saccharomyces cerevisiae Gcs1 is an ADP-ribosylation factor GTPase-activating protein. Poon, P.P., Wang, X., Rotman, M., Huber, I., Cukierman, E., Cassel, D., Singer, R.A., Johnston, G.C. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  9. Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function. Poon, P.P., Cassel, D., Spang, A., Rotman, M., Pick, E., Singer, R.A., Johnston, G.C. EMBO J. (1999) [Pubmed]
  10. Role for Gcs1p in regulation of Arl1p at trans-Golgi compartments. Liu, Y.W., Huang, C.F., Huang, K.B., Lee, F.J. Mol. Biol. Cell (2005) [Pubmed]
  11. The Arf-GTPase-activating protein Gcs1p is essential for sporulation and regulates the phospholipase D Spo14p. Connolly, J.E., Engebrecht, J. Eukaryotic Cell (2006) [Pubmed]
  12. Identification of centaurin-alpha1 as a potential in vivo phosphatidylinositol 3,4,5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating protein, Gcs1. Venkateswarlu, K., Oatey, P.B., Tavaré, J.M., Jackson, T.R., Cullen, P.J. Biochem. J. (1999) [Pubmed]
 
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