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Gene Review

frat1  -  frequently rearranged in advanced T-cell...

Xenopus laevis

 
 
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High impact information on GBP

  • Using a two-hybrid screen, we identified GBP, a maternal Xgsk-3-binding protein that is homologous to a T cell protooncogene in three well-conserved domains [1].
  • Finally, we provide evidence that CK1epsilon stimulates the binding of dishevelled (dsh) to GSk3 binding protein (GBP) in extracts [2].
  • We show that GBP also functions by preventing the GSK-3-mediated phosphorylation of a protein substrate without eliminating its catalytic activity [3].
  • We propose a model in which conventional kinesin transports a GBP-containing complex to the future dorsal side, where GBP dissociates and contributes to the local stabilization of beta-catenin by binding and inhibiting GSK3 [4].
  • Here, we show that the GSK3 inhibitory protein GBP/Frat binds kinesin light chain (KLC), a component of the microtubule motor kinesin [4].
 

Physical interactions of GBP

References

  1. GBP, an inhibitor of GSK-3, is implicated in Xenopus development and oncogenesis. Yost, C., Farr, G.H., Pierce, S.B., Ferkey, D.M., Chen, M.M., Kimelman, D. Cell (1998) [Pubmed]
  2. Physiological regulation of [beta]-catenin stability by Tcf3 and CK1epsilon. Lee, E., Salic, A., Kirschner, M.W. J. Cell Biol. (2001) [Pubmed]
  3. Interaction among GSK-3, GBP, axin, and APC in Xenopus axis specification. Farr, G.H., Ferkey, D.M., Yost, C., Pierce, S.B., Weaver, C., Kimelman, D. J. Cell Biol. (2000) [Pubmed]
  4. GBP binds kinesin light chain and translocates during cortical rotation in Xenopus eggs. Weaver, C., Farr, G.H., Pan, W., Rowning, B.A., Wang, J., Mao, J., Wu, D., Li, L., Larabell, C.A., Kimelman, D. Development (2003) [Pubmed]
  5. Conservation of intracellular Wnt signaling components in dorsal-ventral axis formation in zebrafish. Sumoy, L., Kiefer, J., Kimelman, D. Dev. Genes Evol. (1999) [Pubmed]
 
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