Formins are conserved Rho-GTPase effectors that communicate Rho-GTPase signals to the cytoskeleton. We found that formins were required for the assembly of one of the three budding yeast actin structures: polarized arrays of actin cables. A dominant-active formin induced the assembly of actin cables. The activation and localization of the formin Bni1p required components of the polarisome complex. These findings potentially define the cellular function of formins in budding yeast and explain their involvement in the generation of cell polarity. A requirement for formins in constructing specific actin structures might be the basis for the diverse activities of formins in development.
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Gene/Complex | Qualifier | Gene Ontology Term | Annotation Extension | Evidence | Source | Assigned On |
---|---|---|---|---|---|---|
PEA2 | involved in | regulation of protein localization | has input BNI1 | IMP | SGD | 2014-01-16 |
BNR1 | involved in | formin-nucleated actin cable assembly | IGI with BNI1 | SGD | 2014-01-16 | |
SPA2 | involved in | regulation of protein localization | has input BNI1 | IMP | SGD | 2014-01-16 |
BNI1 | involved in | formin-nucleated actin cable assembly | IGI with BNR1 | SGD | 2014-01-16 | |
BNI1 | involved in | formin-nucleated actin cable assembly | IMP | SGD | 2013-08-07 |
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Gene | Phenotype | Experiment Type | Mutant Information | Strain Background | Chemical | Details |
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BNI1 | actin cytoskeleton morphology: abnormal | classical genetics | activation Allele: BNI1-FΔD C-terminal truncation AA 1751-1953; DAD autoregulatory domain deleted; constitutively active | S288C | Details: dense chaotic network of actin filaments; aberrant disorganized actin cables | |
BNI1 | cell shape: abnormal | classical genetics | activation Allele: BNI1-FΔD C-terminal truncation AA 1751-1953; DAD autoregulatory domain deleted; constitutively active | S288C | Details: cells are large and round, due to defective polarized growth | |
SPA2 | protein/peptide distribution: abnormal Reporter: Bni1p | classical genetics | null Allele: spa2-Δ | S288C | Details: defective recruitment of Bni1p to the bud tip | |
PEA2 | protein/peptide distribution: abnormal Reporter: Bni1p | classical genetics | null Allele: pea2-Δ | S288C | Details: defective recruitment of Bni1p to the bud tip |
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Evidence ID | Analyze ID | Interactor | Interactor Systematic Name | Interactor | Interactor Systematic Name | Allele | Assay | Annotation | Action | Phenotype | SGA score | P-value | Source | Reference | Note |
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Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through the table's pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table; click on the small "i" buttons located within a cell for an annotation to view further details about experiment type and any other genes involved in the interaction.