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Gene Review

COF1  -  cofilin

Saccharomyces cerevisiae S288c

Synonyms: Actin-depolymerizing factor 1, Cofilin, L0596, YLL050C
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Disease relevance of COF1

  • We also demonstrate that cofilin interacts with the large cytoplasmic domains of the alpha1, alpha2 and alpha3 isoforms of Na,K-ATPase, but not with those of glucose transporter 1, glucose transporter 4, cystic fibrosis transmembrane conductance regulator and plasma membrane Ca-ATPase [1].

High impact information on COF1

  • Cofilin promotes rapid actin filament turnover in vivo [2].
  • On the basis of similar results obtained by DAip1 overexpression and effects of latrunculin-A treatment, we propose a function for DAip1 in the control of actin depolymerization in vivo, probably through interaction with cofilin [3].
  • The Ala120-equivalent mutation in yeast cofilin affected cell growth, whereas that of the Phe82-equivalent had no effect in yeast [4].
  • Side chain hydroxyl groups of Ser119, Ser120 and Tyr82 in cofilin form hydrogen bonds with main chain carbonyl moieties from the helix, causing the kink [4].
  • However, fluid phase endocytosis is defective in act1-159 strains. act1-159 is synthetically lethal with cofilin and profilin mutants, supporting the conclusion that mutations in all of these genes impair the polymerization/ depolymerization cycle [5].

Biological context of COF1

  • A complete disruption of the COF1 gene was created in diploid cells [6].
  • Several temperature sensitive (ts-) mutants were independently created by the random mutagenesis of COF1 with hydroxylamine [7].
  • Gene disruption and tetrad analysis showed that gene COF1 is essential for yeast cell growth [8].
  • Isolation of a yeast essential gene, COF1, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein [8].
  • A gene on a multicopy plasmid which suppresses the ts-phenotype of cof1-101, a typical ts-cofilin mutant, was isolated [7].

Anatomical context of COF1


Associations of COF1 with chemical compounds

  • RESULTS: When COF1 was over-expressed in yeast cells under the GAL1 promoter in a medium containing galactose as a sole carbon source, the cells did not survive [7].
  • The NH2-terminal 16kD of Abp1p, a 65-kD yeast protein identified by its ability to bind to actin filaments, is 23% identical to yeast cofilin [6].
  • S3D-cofilin, in which Ser-3 was replaced with Asp, did not bind in vitro to actin while S3A-cofilin did [9].
  • To facilitate the imaging of actin filaments and to avoid the use of rhodamine phalloidin, which competes with cofilin, alpha-actin was labeled with tetramethylrhodamine cadaverine (TRC) at Gln41 [13].
  • However, following the interprotomer cross-linking of Gln41 to Cys374 in F-actin by ANP, cofilin binding did not change FRET from the tryptophan residues to ANP [12].

Physical interactions of COF1

  • Through systematic mutagenesis of Aip1 surfaces, we identify two well-separated F-actin-binding sites, one of which contributes to actin filament binding and disassembly specifically in the presence of cofilin [14].

Regulatory relationships of COF1

  • Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments [14].

Other interactions of COF1

  • In this study, we demonstrate using viscosity, sedimentation, and actin assembly rate assays that yeast cofilin (16 kD) possesses all of these properties [6].
  • Thus, cofilin and Abp1p are structurally related but functionally distinct components of the yeast membrane cytoskeleton [6].
  • Here, we analyze the in vivo function of a ubiquitous actin-interacting protein, Aip1, suggested to work with cofilin [14].
  • In agreement with these observations, we found that like the Arp2/3 complex and the myosins-I, cofilin was essential for the endocytic uptake in vivo, whereas profilin was dispensable [15].
  • S3D-porcine cofilin did not complement the lethality associated with delta cof1 mutations in Saccharomyces cerevisiae while wild-type and S3A-cofilin did [9].

Analytical, diagnostic and therapeutic context of COF1


  1. Identification of the cofilin-binding sites in the large cytoplasmic domain of Na,K-ATPase. Kim, M., Jung, J., Park, C.S., Lee, K. Biochimie (2002) [Pubmed]
  2. Cofilin promotes rapid actin filament turnover in vivo. Lappalainen, P., Drubin, D.G. Nature (1997) [Pubmed]
  3. DAip1, a Dictyostelium homologue of the yeast actin-interacting protein 1, is involved in endocytosis, cytokinesis, and motility. Konzok, A., Weber, I., Simmeth, E., Hacker, U., Maniak, M., Müller-Taubenberger, A. J. Cell Biol. (1999) [Pubmed]
  4. Two activities of cofilin, severing and accelerating directional depolymerization of actin filaments, are affected differentially by mutations around the actin-binding helix. Moriyama, K., Yahara, I. EMBO J. (1999) [Pubmed]
  5. The yeast V159N actin mutant reveals roles for actin dynamics in vivo. Belmont, L.D., Drubin, D.G. J. Cell Biol. (1998) [Pubmed]
  6. Cofilin is an essential component of the yeast cortical cytoskeleton. Moon, A.L., Janmey, P.A., Louie, K.A., Drubin, D.G. J. Cell Biol. (1993) [Pubmed]
  7. Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae. Iida, K., Yahara, I. Genes Cells (1999) [Pubmed]
  8. Isolation of a yeast essential gene, COF1, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein. Iida, K., Moriyama, K., Matsumoto, S., Kawasaki, H., Nishida, E., Yahara, I. Gene (1993) [Pubmed]
  9. Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Moriyama, K., Iida, K., Yahara, I. Genes Cells (1996) [Pubmed]
  10. A coat of filamentous actin prevents clustering of late-endosomal vacuoles in vivo. Drengk, A., Fritsch, J., Schmauch, C., Rühling, H., Maniak, M. Curr. Biol. (2003) [Pubmed]
  11. Identification, characterization, and intracellular distribution of cofilin in Dictyostelium discoideum. Aizawa, H., Sutoh, K., Tsubuki, S., Kawashima, S., Ishii, A., Yahara, I. J. Biol. Chem. (1995) [Pubmed]
  12. Structural effects of cofilin on longitudinal contacts in F-actin. Bobkov, A.A., Muhlrad, A., Kokabi, K., Vorobiev, S., Almo, S.C., Reisler, E. J. Mol. Biol. (2002) [Pubmed]
  13. Severing of F-actin by yeast cofilin is pH-independent. Pavlov, D., Muhlrad, A., Cooper, J., Wear, M., Reisler, E. Cell Motil. Cytoskeleton (2006) [Pubmed]
  14. Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments. Okada, K., Ravi, H., Smith, E.M., Goode, B.L. Mol. Biol. Cell (2006) [Pubmed]
  15. Cofilin, but not profilin, is required for myosin-I-induced actin polymerization and the endocytic uptake in yeast. Idrissi, F.Z., Wolf, B.L., Geli, M.I. Mol. Biol. Cell (2002) [Pubmed]
  16. Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting. Guan, J.Q., Vorobiev, S., Almo, S.C., Chance, M.R. Biochemistry (2002) [Pubmed]
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