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Gene Review

Dstn  -  destrin

Mus musculus

Synonyms: 2610043P17Rik, ADF, AU042046, Actin-depolymerizing factor, Destrin, ...
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Disease relevance of Dstn

  • To directly investigate the role of cofilin activation on the actin cytoskeleton during ischemia, MS1 cells were infected with adenoviruses containing the cDNAs for wild-type Xenopus laevis ADF/cofilin green fluorescent protein [XAC(wt)-GFP], GFP, and the constitutively active and inactive isoforms XAC(S3A)-GFP and XAC(S3E)-GFP [1].
  • RESULTS: In corn1/corn1 mice, focal areas of corneal epithelial hyperplasia alternate with epithelium with normal appearance [2].
  • However, a significant increase of cofilin amount, but not of ADF amount, was observed in these muscles of the dystrophic animals, when the symptom of muscular dystrophy became evident [3].

High impact information on Dstn

  • This review addresses aspects of ADF/cofilin structure, dynamics, regulation and function [4].
  • The actin-depolymerizing factor (ADF)/cofilins are a family of essential actin regulatory proteins, ubiquitous among eukaryotes, that enhance the turnover of actin by regulating the rate constants of polymerization and depolymerization at filament ends, changing the twist of the filament and severing actin filaments [4].
  • The activity of ADF/cofilin is regulated by a variety of mechanisms, including specific phosphorylation and dephosphorylation [4].
  • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function [5].
  • Aberrant actin cytoskeleton leads to accelerated proliferation of corneal epithelial cells in mice deficient for destrin (actin depolymerizing factor) [6].

Biological context of Dstn


Anatomical context of Dstn

  • Actin-depolymerizing factor (ADF)/cofilins are essential regulators of actin filament turnover [9].
  • Cofilin-2 is expressed in muscle cells and ADF is restricted to epithelia and endothelia [9].
  • Cofilin/ADF proteins are a ubiquitously expressed family of F-actin depolymerizing factors found in eukaryotic cells including plants [8].
  • The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration [8].
  • Here we show that mediators of neurodegeneration induce the rapid formation of transient or persistent rod-like inclusions containing ADF/cofilin and actin in axons and dendrites of cultured hippocampal neurons [5].

Associations of Dstn with chemical compounds

  • In higher vertebrates, cells often express as many as three different ADF/cofilin genes and each of these proteins may be phosphorylated on serine 3, giving rise to up to six different species [10].
  • In cultured cells, cofilin, as well as ADF, translocates from the cytoplasm into the nucleus together with actin and forms rod-like structures in response to heat shock or dimethylsulfoxide (DMSO) treatment [11].

Other interactions of Dstn


Analytical, diagnostic and therapeutic context of Dstn

  • Here, Western blotting was used with chemiluminescence substrates of different sensitivities to determine the relative immunoreactivities of different polyclonal rabbit antibodies and a mouse monoclonal antibody to purified ADF/cofilins from plants, protists, nematodes, insects, echinoderms, birds, and mammals [10].
  • Anatomic changes were demonstrated in corn1 and control A.By/SnJ mice from day 10 of gestation of 8 months of age by routine techniques of light microscopic and scanning electron microscopy [14].
  • From immunocross-reactivities and sequence alignments, the principal epitope in mammalian ADF and cofilin-1 recognized by an antibody raised against avian ADF was identified [10].
  • Sequence analysis of mammalian and avian isoforms shows a consistent pattern of charge differences in regions of the protein associated with F-actin-binding that may account for the differences in activity between ADF and cofilin [15].


  1. Cofilin mediates ATP depletion-induced endothelial cell actin alterations. Suurna, M.V., Ashworth, S.L., Hosford, M., Sandoval, R.M., Wean, S.E., Shah, B.M., Bamburg, J.R., Molitoris, B.A. Am. J. Physiol. Renal Physiol. (2006) [Pubmed]
  2. Characterization of Corn1 mice: Alteration of epithelial and stromal cell gene expression. Wang, I., Kao, C.W., Liu, C., Saika, S., Nishina, P.M., Sundberg, J.P., Smith, R.S., Kao, W.W. Mol. Vis. (2001) [Pubmed]
  3. Increased expression of cofilin in dystrophic chicken and mouse skeletal muscles. Hayakawa, K., Minami, N., Ono, S., Ogasawara, Y., Totsuka, T., Abe, H., Tanaka, T., Obinata, T. J. Biochem. (1993) [Pubmed]
  4. Putting a new twist on actin: ADF/cofilins modulate actin dynamics. Bamburg, J.R., McGough, A., Ono, S. Trends Cell Biol. (1999) [Pubmed]
  5. Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Minamide, L.S., Striegl, A.M., Boyle, J.A., Meberg, P.J., Bamburg, J.R. Nat. Cell Biol. (2000) [Pubmed]
  6. Aberrant actin cytoskeleton leads to accelerated proliferation of corneal epithelial cells in mice deficient for destrin (actin depolymerizing factor). Ikeda, S., Cunningham, L.A., Boggess, D., Hawes, N., Hobson, C.D., Sundberg, J.P., Naggert, J.K., Smith, R.S., Nishina, P.M. Hum. Mol. Genet. (2003) [Pubmed]
  7. Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells. Hotulainen, P., Paunola, E., Vartiainen, M.K., Lappalainen, P. Mol. Biol. Cell (2005) [Pubmed]
  8. The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration. Gurniak, C.B., Perlas, E., Witke, W. Dev. Biol. (2005) [Pubmed]
  9. The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics. Vartiainen, M.K., Mustonen, T., Mattila, P.K., Ojala, P.J., Thesleff, I., Partanen, J., Lappalainen, P. Mol. Biol. Cell (2002) [Pubmed]
  10. Cross-reactivity of antibodies to actin- depolymerizing factor/cofilin family proteins and identification of the major epitope recognized by a mammalian actin-depolymerizing factor/cofilin antibody. Shaw, A.E., Minamide, L.S., Bill, C.L., Funk, J.D., Maiti, S., Bamburg, J.R. Electrophoresis (2004) [Pubmed]
  11. Stimulus-dependent disorganization of actin filaments induced by overexpression of cofilin in C2 myoblasts. Ono, S., Abe, H., Obinata, T. Cell Struct. Funct. (1996) [Pubmed]
  12. Spontaneous corneal hem- and lymphangiogenesis in mice with destrin-mutation depend on VEGFR3 signaling. Cursiefen, C., Ikeda, S., Nishina, P.M., Smith, R.S., Ikeda, A., Jackson, D., Mo, J.S., Chen, L., Dana, M.R., Pytowski, B., Kruse, F.E., Streilein, J.W. Am. J. Pathol. (2005) [Pubmed]
  13. beta-Thymosins are not simple actin monomer buffering proteins. Insights from overexpression studies. Sun, H.Q., Kwiatkowska, K., Yin, H.L. J. Biol. Chem. (1996) [Pubmed]
  14. Corn1: a mouse model for corneal surface disease and neovascularization. Smith, R.S., Hawes, N.L., Kuhlmann, S.D., Heckenlively, J.R., Chang, B., Roderick, T.H., Sundberg, J.P. Invest. Ophthalmol. Vis. Sci. (1996) [Pubmed]
  15. Determining the differences in actin binding by human ADF and cofilin. Yeoh, S., Pope, B., Mannherz, H.G., Weeds, A. J. Mol. Biol. (2002) [Pubmed]
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