The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

Svil  -  supervillin

Mus musculus

Synonyms: AU024053, Archvillin, B430302E16Rik, Supervillin, p205/p250
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

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].
  • Transfected protein chimeras containing archvillin insert sequences inhibited myotube formation, consistent with a dominant-negative effect during early myogenesis [2].
  • These data suggest that archvillin is among the first costameric proteins to assemble during myogenesis and that it contributes to myogenic membrane structure and differentiation [2].
  • The membrane skeleton protein supervillin binds tightly to both F-actin and membranes and can potentiate androgen receptor activity in non-muscle cells [2].
 

Biological context of Svil

  • Archvillin cDNAs also contain four exons that encode approximately 47 kDa of additional muscle-specific protein sequence in the form of two inserts within the function-rich N-terminus of supervillin [2].
 

Anatomical context of Svil

  • Striking localizations of archvillin protein and mRNA were observed at the tips of differentiating myotubes [2].
  • Archvillin, like supervillin, binds directly to radiolabeled F-actin and co-fractionates with plasma membranes [2].
  • Colocalization of archvillin with membrane-associated actin filaments, non-muscle myosin II, and--to a lesser extent--vinculin was observed in myoblasts [2].
  • We report that muscle, which constitutes the principal tissue source for supervillin sequences, contains a approximately 250 kDa isoform of supervillin that localizes within nuclei and with dystrophin at costameres, regions of F-actin membrane attachment in skeletal muscle [2].
  • 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. Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton. Oh, S.W., Pope, R.K., Smith, K.P., Crowley, J.L., Nebl, T., Lawrence, J.B., Luna, E.J. J. Cell. Sci. (2003) [Pubmed]
 
WikiGenes - Universities