BOI1 BASIC INFORMATION
| Standard Name | BOI1 |
|---|---|
| Systematic Name | YBL085W |
| Alias | GIN7 , BOB1 |
| Feature Type | ORF, Verified |
| Description | Protein implicated in polar growth, functionally redundant with Boi2p; interacts with bud-emergence protein Bem1p; contains an SH3 (src homology 3) domain and a PH (pleckstrin homology) domain (1 and see Summary Paragraph)
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| Name Description | Bem1 (One) Interacting protein 1 |
| GO Annotations | All BOI1 GO evidence and references |
|---|---|
| View Computational GO annotations for BOI1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Mutant Phenotype | All BOI1 Phenotype details and references |
|---|---|
| Classical genetics | |
| overexpression | |
| Large-scale survey | |
| null | |
| overexpression |
| Interactions | BOI1 All interactions details and references |
|---|---|
| 86 total interaction(s) for 67 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000000181 |
|---|
ADDITIONAL INFORMATION for BOI1
SUMMARY PARAGRAPH for BOI1
The Boi1 protein and its functionally redundant homolog Boi2p have been implicated in actin cytoskeleton reorganization and establishment of cell polarity (2, 3). boi1 boi2 double mutant cells become large and round or lyse with buds, displaying defects in bud formation and in the maintenance of cell polarity (3). Both Boi1p and Boi2p contain SH3, pleckstrin homology (PH), and proline-rich domains. (2, 3) Several structure/function and genetic analysis experiments have been done to determine which domains are important for interactions with other proteins involved in these processes. (2, 3, 4, 5) These studies showed that the Boi proteins interact physically and/or genetically with Bem1p, another SH3 domain protein, as well as three Rho-type GTPases: Cdc42p, Rho3p and the Rho3-related Rho4p (2, 3, 4, 5).
Rho3p/Rho4p interactions: Overexpression of either Rho3p or Rho4p suppresses the synthetic lethality of the boi1 boi2 mutations (2, 3).
Bem1p interactions: Two-hybrid analysis revealed that the proline-rich region of the Boi proteins mediates the interaction with the second SH3 domain of Bem1p (2, 3). Expressing the Boi1 protein with mutations in the proline-rich region suppresses boi1 boi2 double mutants as well as boi1 boi2 bem1 triple mutants (2).
Cdc42p interactions: The PH domain of the Boi proteins is necessary and sufficient for function and mediates the interaction with Cdc42p in the two-hybrid system (2). Additional two-hybrid experiments with Cdc42p point mutants suggest that the Boi proteins interact with the GTP-bound Cdc42p (2). Cells overexpressing Boi1p or Boi2p arrest as large, unbudded cells; cooverexpression of Cdc42p suppresses this defect (3, 6, 2)
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for BOI1]
| 1) | Hallett MA, et al. (2002) Probing the importance and potential roles of the binding of the PH-domain protein Boi1 to acidic phospholipids. BMC Cell Biol 3():16 |
| 2) | Bender L, et al. (1996) Associations among PH and SH3 domain-containing proteins and Rho-type GTPases in Yeast. J Cell Biol 133(4):879-94 |
| 3) | Matsui Y, et al. (1996) Yeast src homology region 3 domain-binding proteins involved in bud formation. J Cell Biol 133(4):865-78 |
| 4) | Chenevert J, et al. (1992) A yeast gene (BEM1) necessary for cell polarization whose product contains two SH3 domains. Nature 356(6364):77-9 |
| 5) | Madden K and Snyder M (1998) Cell polarity and morphogenesis in budding yeast. Annu Rev Microbiol 52():687-744 |
| 6) | Akada R, et al. (1997) Screening and identification of yeast sequences that cause growth inhibition when overexpressed. Mol Gen Genet 254(3):267-74 |




