2000
DOI: 10.1002/1097-0177(2000)9999:9999<::aid-dvdy1017>3.0.co;2-9
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Interaction of Frizzled 7 and Dishevelled inXenopus

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Cited by 32 publications
(8 citation statements)
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“…The intracellular domain of BAMBI is important for the interaction with all three proteins while the extracellular domain can associate only with Fzd, which is consistent with the topological structure of BAMBI as a single-spanned transmembrane protein. It has been demonstrated that Wnt treatment results in the plasma membrane recruitment of Dvl (34), but the binding of Dvl to Fzd could be relatively weak (40). Our data uncovered that BAMBI can increase the interaction between Fzd and Dvl as this interaction became detectable only in the presence of BAMBI in our experimental condition (Fig.…”
Section: Discussionmentioning
confidence: 81%
See 1 more Smart Citation
“…The intracellular domain of BAMBI is important for the interaction with all three proteins while the extracellular domain can associate only with Fzd, which is consistent with the topological structure of BAMBI as a single-spanned transmembrane protein. It has been demonstrated that Wnt treatment results in the plasma membrane recruitment of Dvl (34), but the binding of Dvl to Fzd could be relatively weak (40). Our data uncovered that BAMBI can increase the interaction between Fzd and Dvl as this interaction became detectable only in the presence of BAMBI in our experimental condition (Fig.…”
Section: Discussionmentioning
confidence: 81%
“…Wnt signal is propagated following the binding of Wnt ligands to a hetero-oligomeric receptor complex consisting of Fzd and LRP5/6 (29 -31), which results in the recruitment of Axin to LRP (32,33) and Dvl to Fzd (29,34). However, the interaction between Dvl and Frizzled is apparently weak, and it is unclear whether other proteins are involved in this process.…”
Section: Bambi Enhances the Interaction Of Fzd5 And Dvl2-thementioning
confidence: 99%
“…pCS2+ xFz7 encodes the full-length xFz7 (Medina and Steinbeisser, 2000). pCS2+ ΔCxFz7 lacks the 26 C-terminal amino acids, pCS2+ NxFz7-fun comprises the N-terminal domain of xFz7 fused with a fun domain (Medina et al, 2000), and pCS2+ ΔNxFz7 encodes the seven transmembrane domains and the C tail of xFz7 (Winklbauer et al, 2001).…”
Section: Methodsmentioning
confidence: 99%
“…Here, we show that Dpr1 interacts with Dvl and enhances Dvl degradation in a lysosome inhibitorsensitive and proteasome inhibitor-insensitive manner in an analogous way to the activity of Dpr2 that associates with transforming growth factor-␤ type I receptors and targets them for lysosomal degradation (10). Dvl shuttles between the cytoplasm and the nucleus (22) and can also be recruited to the plasma membrane (23,24). How Dpr1 promotes Dvl degradation awaits further investigation.…”
Section: Interaction Between Mammalian Dpr1 and Dvl At The Endogenousmentioning
confidence: 98%