BNI1 Antibody

1. We studied the interactions between actin and the FH2 domains of formins Cdc12, Bni1 and mDia1 to understand the factors underlying their different rates of polymerization. All-atom molecular dynamics simulations revealed two factors that influence actin filament elongation and correlate with the rates of elongation PMID: 30035712
2. Expression of a hyperactive variant of Bni1 (Bni1-V360D) rescues these defects and partially restores proper spindle positioning in the mutant, suggesting that the failure of dma1 dma2 mutant cells to position the spindle is partly due to faulty formin activity. PMID: 27449057
3. four regions in Bni1p that contribute to its localization to the bud and at the bud neck were difined PMID: 22160598
4. crystal structure of the yeast Bni1p FH2 domain in complex with tetramethylrhodamine-actin PMID: 15635372
5. temperature-sensitive growth phenotype of the bni1Delta sla2-82 mutant was suppressed by increased expression of ACT1 PMID: 16547104
6. Mutations that impair the actin assembly activity of Bni1 abolished the movement of Bni1 speckles, even when actin cables were present. PMID: 17344480
7. During actin filament elongation, formin FH1 domains bind profilin-actin complexes and deliver them rapidly to the barbed end associated with the FH2 domain. PMID: 18160294

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KEGG: sce:YNL271C

STRING: 4932.YNL271C