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Gene Review

SAC6  -  fimbrin

Saccharomyces cerevisiae S288c

Synonyms: ABP67, Fimbrin, YD9302.04C, YDR129C
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High impact information on SAC6

  • Thus Sac6p binds to actin in vitro, and functionally associates with actin structures involved in the development and maintenance of cell polarity in vivo [1].
  • Requirement of yeast fimbrin for actin organization and morphogenesis in vivo [1].
  • We report here that Sac6p is an actin-filament bundling protein 43% identical in amino-acid sequence to the vertebrate bundling protein fimbrin [1].
  • In addition, synthetic-lethal interactions were observed for double-mutants containing null alleles of SLA2 and SAC6 [2].
  • We demonstrate that the human T- and L-fimbrins, in addition to complementing the temperature-sensitive growth defect of the sac6 null mutant, restore both normal cytoskeletal organization and cell shape to the mutant cells [3].

Biological context of SAC6


Anatomical context of SAC6

  • Second, the lack of structural and functional homology among these genetically redundant proteins (fimbrin and capping protein or Abp1p) indicates that they regulate the actin cytoskeleton by different mechanisms [4].

Associations of SAC6 with chemical compounds

  • After digestion of the 60 kDa fragment with cyanogen bromide, the N-terminal 21-amino acid sequence of one of the resulting peptides was found to show sequence similarity to a region near the actin-binding site (amino acid residues 260-281) of yeast fimbrin [9].

Physical interactions of SAC6

  • To examine the mechanism of suppression, we have sequenced 17 sac6 suppressor alleles, and found that they change nine different residues, all of which cluster in three regions of one of the two actin-binding domains of Sac6p [10].

Regulatory relationships of SAC6

  • Previously, we showed that actin mutations that are suppressed by sac6 mutations encode proteins with a reduced affinity for wild-type Sac6p [11].

Other interactions of SAC6

  • Together, these observations identify a likely site of interaction of fimbrin on actin [12].
  • Double mutants lacking fimbrin and either Abp1p or capping protein show negative synthetic effects on growth, in the most extreme case resulting in lethality [4].
  • Also, synthetic lethality between anc3 and sac6 mutations, and between anc4 and tpm1 mutations was observed [13].
  • In addition, synthetic growth defects were observed between null alleles of GCS1 and SAC6, the gene encoding the yeast fimbrin homologue [14].

Analytical, diagnostic and therapeutic context of SAC6

  • Sequence analysis indicates that all of these mutations change residues that cluster in the small domain of the actin crystal structure, suggesting that this region is an important part of the Sac6p-binding domain [12].


  1. Requirement of yeast fimbrin for actin organization and morphogenesis in vivo. Adams, A.E., Botstein, D., Drubin, D.G. Nature (1991) [Pubmed]
  2. Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae. Holtzman, D.A., Yang, S., Drubin, D.G. J. Cell Biol. (1993) [Pubmed]
  3. Isoform-specific complementation of the yeast sac6 null mutation by human fimbrin. Adams, A.E., Shen, W., Lin, C.S., Leavitt, J., Matsudaira, P. Mol. Cell. Biol. (1995) [Pubmed]
  4. Unexpected combinations of null mutations in genes encoding the actin cytoskeleton are lethal in yeast. Adams, A.E., Cooper, J.A., Drubin, D.G. Mol. Biol. Cell (1993) [Pubmed]
  5. Calcium-independent calmodulin requirement for endocytosis in yeast. Kübler, E., Schimmöller, F., Riezman, H. EMBO J. (1994) [Pubmed]
  6. Dominant suppressors of yeast actin mutations that are reciprocally suppressed. Adams, A.E., Botstein, D. Genetics (1989) [Pubmed]
  7. The role of T-fimbrin in the response to DNA damage: silencing of T-fimbrin by small interfering RNA sensitizes human liver cancer cells to DNA-damaging agents. Ikeda, H., Sasaki, Y., Kobayashi, T., Suzuki, H., Mita, H., Toyota, M., Itoh, F., Shinomura, Y., Tokino, T., Imai, K. Int. J. Oncol. (2005) [Pubmed]
  8. Use of a synthetic lethal screen to identify yeast mutants impaired in endocytosis, vacuolar protein sorting and the organization of the cytoskeleton. Singer-Krüger, B., Ferro-Novick, S. Eur. J. Cell Biol. (1997) [Pubmed]
  9. A new Tetrahymena actin-binding protein is localized in the division furrow. Watanabe, A., Kurasawa, Y., Watanabe, Y., Numata, O. J. Biochem. (1998) [Pubmed]
  10. Genetic analysis of the fimbrin-actin binding interaction in Saccharomyces cerevisiae. Brower, S.M., Honts, J.E., Adams, A.E. Genetics (1995) [Pubmed]
  11. Allele-specific suppression by formation of new protein-protein interactions in yeast. Sandrock, T.M., O'Dell, J.L., Adams, A.E. Genetics (1997) [Pubmed]
  12. Actin mutations that show suppression with fimbrin mutations identify a likely fimbrin-binding site on actin. Honts, J.E., Sandrock, T.S., Brower, S.M., O'Dell, J.L., Adams, A.E. J. Cell Biol. (1994) [Pubmed]
  13. Genetic evidence for functional interactions between actin noncomplementing (Anc) gene products and actin cytoskeletal proteins in Saccharomyces cerevisiae. Vinh, D.B., Welch, M.D., Corsi, A.K., Wertman, K.F., Drubin, D.G. Genetics (1993) [Pubmed]
  14. GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro. Blader, I.J., Cope, M.J., Jackson, T.R., Profit, A.A., Greenwood, A.F., Drubin, D.G., Prestwich, G.D., Theibert, A.B. Mol. Biol. Cell (1999) [Pubmed]
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