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Gene Review

Sorbs3  -  sorbin and SH3 domain containing 3

Mus musculus

Synonyms: SCAM-1, SH3 domain-containing protein SH3P3, SH3-containing adapter molecule 1, SH3P3, Scam1, ...
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Disease relevance of Sorbs3

  • Here, we show that vinexin beta increases the amount of and reduces the mobility on SDS-PAGE of Wiskott-Aldrich syndrome protein family verprolin-homologous protein (WAVE) 2 protein, which is a key factor modulating actin polymerization in migrating cells [1].

High impact information on Sorbs3


Biological context of Sorbs3


Anatomical context of Sorbs3


Associations of Sorbs3 with chemical compounds


Physical interactions of Sorbs3

  • We report the identification of the cytoskeletal protein Vinexin as a protein interacting with SHIP2 [7].

Enzymatic interactions of Sorbs3


Regulatory relationships of Sorbs3

  • The dominant-negative mutant of vinexin beta inhibited the anchorage-independent ERK2 activation induced by the PKA inhibitor [6].
  • Ultimately, Sox9 transcription was induced by Vinexin gamma [5].
  • Our data suggest that SHIP2 interaction with Vinexin promotes the localization of SHIP2 at the periphery of the cells leaving its catalytic site intact [7].
  • These results suggest that vinexin beta regulates the proteasome-dependent degradation of WAVE2 in a PKA-dependent manner [1].

Other interactions of Sorbs3


Analytical, diagnostic and therapeutic context of Sorbs3

  • Using whole-mount in situ hybridization, we showed here that expression of vinexin alpha, the longer vinexin transcript, is strictly regulated, although the shorter transcript, vinexin beta, is expressed almost ubiquitously during embryonic development in mice [4].
  • By Northern blotting, we identified two types of vinexin mRNA that were 3 and 2 kb in length [2].
  • Whatever the final answer turns out to be, the genetic dissection of the SCAM superfamilies has led to a much better understanding of the different steps required to form, differentiate and modify a synapse [11].


  1. Protein kinase A-dependent increase in WAVE2 expression induced by the focal adhesion protein vinexin. Mitsushima, M., Sezaki, T., Akahane, R., Ueda, K., Suetsugu, S., Takenawa, T., Kioka, N. Genes Cells (2006) [Pubmed]
  2. Vinexin: a novel vinculin-binding protein with multiple SH3 domains enhances actin cytoskeletal organization. Kioka, N., Sakata, S., Kawauchi, T., Amachi, T., Akiyama, S.K., Okazaki, K., Yaen, C., Yamada, K.M., Aota, S. J. Cell Biol. (1999) [Pubmed]
  3. Vinexin beta interacts with the non-phosphorylated AF-1 domain of retinoid receptor gamma (RARgamma) and represses RARgamma-mediated transcription. Bour, G., Plassat, J.L., Bauer, A., Lalevée, S., Rochette-Egly, C. J. Biol. Chem. (2005) [Pubmed]
  4. Expression of vinexin alpha in the dorsal half of the eye and in the cardiac outflow tract and atrioventricular canal. Kawauchi, T., Ikeya, M., Takada, S., Ueda, K., Shirai, M., Takihara, Y., Kioka, N., Amachi, T. Mech. Dev. (2001) [Pubmed]
  5. A novel isoform of Vinexin, Vinexin gamma, regulates Sox9 gene expression through activation of MAPK cascade in mouse fetal gonad. Matsuyama, M., Mizusaki, H., Shimono, A., Mukai, T., Okumura, K., Abe, K., Shimada, K., Morohashi, K. Genes Cells (2005) [Pubmed]
  6. Vinexin beta regulates the anchorage dependence of ERK2 activation stimulated by epidermal growth factor. Suwa, A., Mitsushima, M., Ito, T., Akamatsu, M., Ueda, K., Amachi, T., Kioka, N. J. Biol. Chem. (2002) [Pubmed]
  7. SHIP2 interaction with the cytoskeletal protein Vinexin. Paternotte, N., Zhang, J., Vandenbroere, I., Backers, K., Blero, D., Kioka, N., Vanderwinden, J.M., Pirson, I., Erneux, C. FEBS J. (2005) [Pubmed]
  8. Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin. Mitsushima, M., Suwa, A., Amachi, T., Ueda, K., Kioka, N. J. Biol. Chem. (2004) [Pubmed]
  9. Abl kinase interacts with and phosphorylates vinexin. Mitsushima, M., Takahashi, H., Shishido, T., Ueda, K., Kioka, N. FEBS Lett. (2006) [Pubmed]
  10. Role of interaction with vinculin in recruitment of vinexins to focal adhesions. Takahashi, H., Mitsushima, M., Okada, N., Ito, T., Aizawa, S., Akahane, R., Umemoto, T., Ueda, K., Kioka, N. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  11. The resilient synapse: insights from genetic interference of synaptic cell adhesion molecules. Piechotta, K., Dudanova, I., Missler, M. Cell Tissue Res. (2006) [Pubmed]
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