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

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Gene Review: 

SVIL  -  supervillin

Bos taurus

 
 
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High impact information on SVIL

  • TRIP6 partially rescues SV effects on stress fibers and FAs, apparently by mislocating SV away from FAs [1].
  • Supervillin modulation of focal adhesions involving TRIP6/ZRP-1 [1].
  • Membrane skeleton proteins include fodrin (nonerythroid spectrin), myosin-IIA, myosin-IG, alpha-actinin 1, alpha-actinin 4, vimentin, and the F-actin-binding protein, supervillin [2].
  • In spreading neutrophils, supervillin localizes with F-actin in cell extensions and in discrete basal puncta that partially overlap with Galpha(i) staining [2].
 

Anatomical context of SVIL

  • We show that supervillin (SV)--a peripheral membrane protein that binds myosin II and F-actin in such cells--negatively regulates stress fibers, FAs, and cell-substrate adhesion [1].

References

  1. Supervillin modulation of focal adhesions involving TRIP6/ZRP-1. Takizawa, N., Smith, T.C., Nebl, T., Crowley, J.L., Palmieri, S.J., Lifshitz, L.M., Ehrhardt, A.G., Hoffman, L.M., Beckerle, M.C., Luna, E.J. J. Cell Biol. (2006) [Pubmed]
  2. Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes. Nebl, T., Pestonjamasp, K.N., Leszyk, J.D., Crowley, J.L., Oh, S.W., Luna, E.J. J. Biol. Chem. (2002) [Pubmed]
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