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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

TWF1  -  Twf1p

Saccharomyces cerevisiae S288c

Synonyms: Twinfilin-1, Twinfilin-A, YGR080W
 
 
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High impact information on TWF1

  • Consistently, in vivo twinfilin localizes to actin tails of propelling endosomes [1].
  • Native gel assays demonstrate that twinfilin binds ADP-actin monomers with higher affinity than ATP-actin monomers [2].
  • A6/twinfilin mRNA is expressed in most adult tissues but not in skeletal muscle and spleen [3].
 

Associations of TWF1 with chemical compounds

 

Other interactions of TWF1

  • Based on these results, we propose a model for the biological role of twinfilin as a protein that localizes actin monomers to the sites of rapid filament assembly in cells [2].
 

Analytical, diagnostic and therapeutic context of TWF1

  • Furthermore, site-directed mutagenesis studies revealed that the CP-binding site resides in the conserved C-terminal tail region of twinfilin [4].

References

  1. Mammalian twinfilin sequesters ADP-G-actin and caps filament barbed ends: implications in motility. Helfer, E., Nevalainen, E.M., Naumanen, P., Romero, S., Didry, D., Pantaloni, D., Lappalainen, P., Carlier, M.F. EMBO J. (2006) [Pubmed]
  2. Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin. Palmgren, S., Ojala, P.J., Wear, M.A., Cooper, J.A., Lappalainen, P. J. Cell Biol. (2001) [Pubmed]
  3. Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics. Vartiainen, M., Ojala, P.J., Auvinen, P., Peränen, J., Lappalainen, P. Mol. Cell. Biol. (2000) [Pubmed]
  4. Biological role and structural mechanism of twinfilin-capping protein interaction. Falck, S., Paavilainen, V.O., Wear, M.A., Grossmann, J.G., Cooper, J.A., Lappalainen, P. EMBO J. (2004) [Pubmed]
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