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Gene Review

BNI1  -  Bni1p

Saccharomyces cerevisiae S288c

Synonyms: N0646, PPF3, Pointed projection formation protein 3, Protein BNI1, SHE5, ...
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High impact information on BNI1

  • We used total internal reflection fluorescence microscopy to observe directly individual actin filament polymerization in the presence of two mammalian formins (mDia1 and mDia2) and two yeast formins (Bni1p and Cdc12p) [1].
  • The Saccharomyces cerevisiae BNI1 gene product (Bni1p) is a member of the formin family of proteins, which participate in cell polarization, cytokinesis, and vertebrate limb formation [2].
  • During mating pheromone response, bni1 mutants showed defects both in polarized morphogenesis and in reorganization of the underlying actin cytoskeleton [2].
  • Pheromone-induced polarization is dependent on the Fus3p MAPK acting through the formin Bni1p [3].
  • These data suggest a model wherein activated Fus3p is recruited back to the cortex, where it activates Bni1p to promote polarization and cell fusion [3].

Biological context of BNI1

  • This phenotype is similar to that previously observed in cells lacking the kinesin Kip3p and, in fact, BNI1 and KIP3 were found to be in the same genetic pathway [4].
  • Bni1p shares the FH1 and FH2 domains with proteins involved in cytokinesis or establishment of cell polarity [5].
  • Bni1p fused with green fluorescent protein localized to the sites of cell growth throughout the cell cycle [6].
  • A bni1-disrupted cell showed a defect in directed growth to the pre-bud site and to the bud tip (apical growth), causing its abnormally spherical cell shape and thick bud neck [6].
  • Together, these results suggest that one function of Ste20p may be to activate the polarisome complex by phosphorylation of Bni1p [7].

Anatomical context of BNI1


Associations of BNI1 with chemical compounds

  • EF1alpha bound to the 186 amino acids region of Bni1p, located between the FH1 domain, the proline-rich profilin-binding domain, and the FH2 domain, of which function is not known [8].
  • Introduction of constitutively active ras1G13V in the bni1 strain or addition of cyclic AMP to the growth medium did not bypass bni1 hyphal growth defects [11].

Physical interactions of BNI1

  • Moreover, yeast two-hybrid and biochemical studies demonstrate that Bni1p and Bnr1p interact directly with profilin at the FH1 domains [5].
  • The BNI1 gene deleted in the EF1alpha-binding region did not suppress the bni1 bnr1 mutation in which the actin organization was impaired [8].
  • We mapped Bud6 binding activity to specific residues in the carboxyl terminus of Bni1 that are adjacent to its diaphanous autoregulatory domain (DAD) [12].

Regulatory relationships of BNI1

  • Bni1p stimulates actin polymerization for the formation of actin cables [13].
  • Ras1-induced hyphal development in Candida albicans requires the formin Bni1 [11].
  • We show that the essential function of Rho3p and Rho4p is to activate the formins Bni1p and Bnr1p, and that activated alleles of either formin are able to bypass the requirement for these Rho proteins [14].

Other interactions of BNI1

  • Cells of the bni1 bnr1 mutant arrested at the restrictive temperature are deficient in bud emergence, exhibit a random distribution of cortical actin patches and often become multinucleate [5].
  • Disruption of BNI1 or BNR1 does not show any deleterious effect on cell growth, but the bni1 bnr1 mutant shows a severe temperature-sensitive growth phenotype [5].
  • We have recently shown that Bni1p is a potential target of Rho1p [5].
  • Genetic analysis placed BNI1 in the KAR9 pathway for nuclear migration [15].
  • BNI1 was originally identified on the basis of genetic interaction with CDC12, which encodes one of the neck-filament-associated septin proteins, suggesting that these proteins may be involved in positioning the bipolar signals [16].

Analytical, diagnostic and therapeutic context of BNI1


  1. Control of the assembly of ATP- and ADP-actin by formins and profilin. Kovar, D.R., Harris, E.S., Mahaffy, R., Higgs, H.N., Pollard, T.D. Cell (2006) [Pubmed]
  2. Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Evangelista, M., Blundell, K., Longtine, M.S., Chow, C.J., Adames, N., Pringle, J.R., Peter, M., Boone, C. Science (1997) [Pubmed]
  3. Pheromone-induced polarization is dependent on the Fus3p MAPK acting through the formin Bni1p. Matheos, D., Metodiev, M., Muller, E., Stone, D., Rose, M.D. J. Cell Biol. (2004) [Pubmed]
  4. Control of mitotic spindle position by the Saccharomyces cerevisiae formin Bni1p. Lee, L., Klee, S.K., Evangelista, M., Boone, C., Pellman, D. J. Cell Biol. (1999) [Pubmed]
  5. Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. Imamura, H., Tanaka, K., Hihara, T., Umikawa, M., Kamei, T., Takahashi, K., Sasaki, T., Takai, Y. EMBO J. (1997) [Pubmed]
  6. Dynamic localization and function of Bni1p at the sites of directed growth in Saccharomyces cerevisiae. Ozaki-Kuroda, K., Yamamoto, Y., Nohara, H., Kinoshita, M., Fujiwara, T., Irie, K., Takai, Y. Mol. Cell. Biol. (2001) [Pubmed]
  7. Synthetic lethal analysis implicates Ste20p, a p21-activated potein kinase, in polarisome activation. Goehring, A.S., Mitchell, D.A., Tong, A.H., Keniry, M.E., Boone, C., Sprague, G.F. Mol. Biol. Cell (2003) [Pubmed]
  8. Interaction of Rho1p target Bni1p with F-actin-binding elongation factor 1alpha: implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae. Umikawa, M., Tanaka, K., Kamei, T., Shimizu, K., Imamura, H., Sasaki, T., Takai, Y. Oncogene (1998) [Pubmed]
  9. Interactions of elongation factor 1alpha with F-actin and beta-actin mRNA: implications for anchoring mRNA in cell protrusions. Liu, G., Grant, W.M., Persky, D., Latham, V.M., Singer, R.H., Condeelis, J. Mol. Biol. Cell (2002) [Pubmed]
  10. Identification of novel mutations in ACT1 and SLA2 that suppress the actin-cable-overproducing phenotype caused by overexpression of a dominant active form of Bni1p in Saccharomyces cerevisiae. Yoshiuchi, S., Yamamoto, T., Sakane, H., Kadota, J., Mochida, J., Asaka, M., Tanaka, K. Genetics (2006) [Pubmed]
  11. Ras1-induced hyphal development in Candida albicans requires the formin Bni1. Martin, R., Walther, A., Wendland, J. Eukaryotic Cell (2005) [Pubmed]
  12. Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6. Moseley, J.B., Goode, B.L. J. Biol. Chem. (2005) [Pubmed]
  13. Septin ring assembly requires concerted action of polarisome components, a PAK kinase Cla4p, and the actin cytoskeleton in Saccharomyces cerevisiae. Kadota, J., Yamamoto, T., Yoshiuchi, S., Bi, E., Tanaka, K. Mol. Biol. Cell (2004) [Pubmed]
  14. Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast. Dong, Y., Pruyne, D., Bretscher, A. J. Cell Biol. (2003) [Pubmed]
  15. The cortical localization of the microtubule orientation protein, Kar9p, is dependent upon actin and proteins required for polarization. Miller, R.K., Matheos, D., Rose, M.D. J. Cell Biol. (1999) [Pubmed]
  16. Genetic analysis of the bipolar pattern of bud site selection in the yeast Saccharomyces cerevisiae. Zahner, J.E., Harkins, H.A., Pringle, J.R. Mol. Cell. Biol. (1996) [Pubmed]
  17. Rho1p-Bni1p-Spa2p interactions: implication in localization of Bni1p at the bud site and regulation of the actin cytoskeleton in Saccharomyces cerevisiae. Fujiwara, T., Tanaka, K., Mino, A., Kikyo, M., Takahashi, K., Shimizu, K., Takai, Y. Mol. Biol. Cell (1998) [Pubmed]
  18. Saccharomyces cerevisiae MATa mutant cells defective in pointed projection formation in response to alpha-factor at high concentrations. Yorihuzi, T., Ohsumi, Y. Yeast (1994) [Pubmed]
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