LAS17/YOR181W Summary 
LAS17 BASIC INFORMATION
| Standard Name | LAS17 |
|---|---|
| Systematic Name | YOR181W |
| Alias | BEE1 1 |
| Feature Type | ORF, Verified |
| Description | Actin assembly factor, activates the Arp2/3 protein complex that nucleates branched actin filaments; localizes with the Arp2/3 complex to actin patches; homolog of the human Wiskott-Aldrich syndrome protein (WASP) (1, 2 and see Summary Paragraph) 
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| Name Description | Local Anestheticum Sensitive 3 |
| GO Annotations | All LAS17 GO evidence and references |
|---|---|
| View Computational GO annotations for LAS17 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Mutant Phenotype | All LAS17 Phenotype details and references |
|---|---|
| Classical genetics | |
| conditional | |
| null |
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| overexpression | |
| Large-scale survey | |
| null | |
| overexpression |
| Interactions | LAS17 All interactions details and references |
|---|---|
| 206 total interaction(s) for 73 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 |
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| Primary SGDID | S000005707 |
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LAS17 RESOURCES
| SGD ORF map | GBrowse |
|---|---|
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Click on histogram for expression summary
Expression Summary
ADDITIONAL INFORMATION for LAS17
SUMMARY PARAGRAPH for LAS17
Las17p/Bee1p is an activator of the Arp2/3 protein complex that nucleates branched actin filaments. It is the only S. cerevisiae homolog of the human Wiskott-Aldrich syndrome protein (WASP) (4, 1) and is a member of the larger WASP/SCAR/WAVE protein family. Las17p was identified biochemically as an essential nucleation factor in the reconstitution of cortical actin patches in vitro, and independently as a verprolin (Vrp1p/End5p)-interacting protein (5, 6). Las17p localizes with the Arp2/3 complex to actin patches, and disruption of LAS17 leads to the loss of actin patches and a block in endocytosis (1, 6, 7).
Las17p physically interacts with the Arp2/3 complex. This interaction requires the carboxy-terminal WA (WH2 [WASp homology 2] and A[acidic]) domain of Las17p and is dependent upon two subunits of the Arp2/3 complex, Arc15p and Arc19p (2). The WA domain is sufficient for Arp2/3 complex binding and activation in vitro (2). The WA domain shares sequence similarity and genetic redundancy with an acidic domain in myosin I (Myo3p and Myo5p in S. cerevisiae), which also interacts with the Arp2/3 complex (8). These proteins appear to function redundantly in the activation of the Arp2/3 complex, as combined deletions of the WA domain of Las17p and the type I myosins abolish actin nucleation at cortical actin patches (4).
Genetic and biochemical studies have identified numerous proteins that physically interact with Las17p. The WH1 domain of Las17p binds strongly to verprolin (Vrp1p/End5p), the yeast homolog of human WIP (WASP-interacting protein), which is involved in Las17p localization (9, 10). The proline-rich region of Las17p binds to SH3 domain-containing proteins, including Sla1p (an actin patch protein with a role in endocytosis), Bbc1p/Mti1p, Bzz1p/Lsb7p, Myo3p, Myo5p, Lsb1p, Lsb2p, Ysc84p, Sho1p, and Rvs167p (11, 1, 7, 12, 4, 13). Although the significance of many of these interactions is not known, they may regulate the activity of Las17p, and thus, the activity of the Arp2/3 complex. Unlike other WASP family members, Las17p does not contain a conserved Cdc42p-binding domain and does not appear to be regulated by auto-inhibition (11).
Last updated: 2003-12-19
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for LAS17]
| 1) | Li R (1997) Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton. J Cell Biol 136(3):649-58 |
| 2) | Winter D, et al. (1999) Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr Biol 9(9):501-4 |
| 3) | Tohe A and Oguchi T (1998) Isolation and characterization of the yeast las21 mutants, which are sensitive to a local anestheticum, tetracaine. Genes Genet Syst 73(6):365-75 |
| 4) | Lechler T, et al. (2000) Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J Cell Biol 148(2):363-73 |
| 5) | Lechler T and Li R (1997) In vitro reconstitution of cortical actin assembly sites in budding yeast. J Cell Biol 138(1):95-103 |
| 6) | Naqvi SN, et al. (1998) The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast. Curr Biol 8(17):959-62 |
| 7) | Madania A, et al. (1999) The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex. Mol Biol Cell 10(10):3521-38 |
| 8) | Evangelista M, et al. (2000) A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. J Cell Biol 148(2):353-62 |
| 9) | Lechler T, et al. (2001) A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast. J Cell Biol 155(2):261-70 |
| 10) | Vaduva G, et al. (1997) Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton. J Cell Biol 139(7):1821-33 |
| 11) | Rodal AA, et al. (2003) Negative regulation of yeast WASp by two SH3 domain-containing proteins. Curr Biol 13(12):1000-8 |
| 12) | Drees BL, et al. (2001) A protein interaction map for cell polarity development. J Cell Biol 154(3):549-71 |
| 13) | Tong AH, et al. (2002) A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules. Science 295(5553):321-4 |
