| Standard Name | GCS1 1 |
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| Systematic Name | YDL226C |
| Feature Type | ORF, Verified |
| Description | ADP-ribosylation factor GTPase activating protein (ARF GAP); involved in ER-Golgi transport; shares functional similarity with Glo3p; GCS1 has a paralog, SPS18, that arose from the whole genome duplication (2, 3, 4 and see Summary Paragraph) |
| Name Description | Growth Cold Sensitive 5 |
| Chromosomal Location | |
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| Note: this feature is encoded on the Crick strand. | |
| View Computational GO annotations for GCS1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| 261 total interaction(s) for 148 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
| Note: this feature is encoded on the Crick strand. | |||||||||||||
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
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| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000002385 |
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GCS1 encodes a GTPase activating protein (GAP) for ADP ribosylation factors (ARFs, encoded by ARF1, ARF2, and ARF3 in yeast), and interacts genetically with ARF1 and ARF2 (6). ARFs are GTPases of the Ras superfamily that regulate the formation of coated vesicles in intracellular trafficking (7, 8). The process of vesicle formation in the exocytic and endocytic pathways has been recently reviewed (9), as has the role of ARF (10).
GCS1 was originally identified as a gene required for cells to reenter the mitotic cell cycle from stationary phase (5, 1). Gcs1p binds actin in vitro, and may interact with the cytoskeleton in vivo. Disruption of GCS1 causes cytoskeletal defects, and GCS1 and shows genetic interactions with SLA2 and SAC6, which encode actin binding proteins (11). A second ARF GAP, Glo3p, has been identified in yeast; a gcs1 glo3 double deletion is inviable (12). Genetic interactions with BET1, BOS1, and SEC22, which encode v-SNARES, implicate Gcs1p and Glo3p in transport between the ER and the Golgi (12). A protein with sequence similarity to Gcs1p, centaurin alpha, has been found in rat and human (13).
| 1) | Ireland LS, et al. (1994) A member of a novel family of yeast 'zn-finger' proteins mediates the transition from stationary phase to cell proliferation. EMBO J 13(16):3812-21 |
| 2) | Poon PP, et al. (2001) Expression, analysis, and properties of yeast ADP-ribosylation factor (ARF) GTPase activating proteins (GAPs) Gcs1 and Glo3. Methods Enzymol 329:317-24 |
| 3) | Poon PP, et al. (2001) The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function for transport from the yeast trans-Golgi network. J Cell Biol 155(7):1239-50 |
| 4) | Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 |
| 5) | Drebot MA, et al. (1987) A yeast mutant conditionally defective only for reentry into the mitotic cell cycle from stationary phase. Proc Natl Acad Sci U S A 84(22):7948-52 |
| 6) | Poon PP, et al. (1996) Saccharomyces cerevisiae Gcs1 is an ADP-ribosylation factor GTPase-activating protein. Proc Natl Acad Sci U S A 93(19):10074-7 |
| 7) | Moss J and Vaughan M (1998) Molecules in the ARF orbit. J Biol Chem 273(34):21431-4 |
| 8) | Moss J and Vaughan M (1999) Activation of toxin ADP-ribosyltransferases by eukaryotic ADP-ribosylation factors. Mol Cell Biochem 193(1-2):153-7 |
| 9) | Springer S, et al. (1999) A primer on vesicle budding. Cell 97(2):145-8 |
| 10) | Roth MG (1999) Snapshots of ARF1: implications for mechanisms of activation and inactivation. Cell 97(2):149-52 |
| 11) | Blader IJ, et al. (1999) 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. Mol Biol Cell 10(3):581-96 |
| 12) | Poon PP, et al. (1999) Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function. EMBO J 18(3):555-64 |
| 13) | Venkateswarlu K, et al. (1999) 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. Biochem J 340 ( Pt 2)():359-63 |





