Search results for LRP6

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Reaction (4 results from a total of 22)

Identifier: R-HSA-4641249
Species: Homo sapiens
Compartment: plasma membrane
ZNFR3 and RNF43 are plasma membrane E3 RING domain ubiquitin ligases that have been shown to ubiquitinate FZD proteins to promote their downregulation (Hao et al, 2012). Inhibition of ZNRF3 or RNF43 increases the protein level of FZD and LRP6 at the plasma membrane, and stably expressed ZNRF3 can be co-immunoprecipitated with endogenous LRP6 and FZD6 (Hao et al, 2012; Jiang et al 2013). Turnover of the LRP6 and FZD receptors appears to be regulated by multiubiquitination and is abrogated upon treatment with lysosomal inhibitors (Mukai et al, 2010).
Identifier: R-HSA-4641253
Species: Homo sapiens
Compartment: plasma membrane
ZNRF3 has been shown to ubiquitinate FZD4 in vivo, and inhibition of ZNRF3/RNF43 increases the protein levels of LRP6 and FZD8 at the cell surface (Hao et al, 2012; Jiang et al, 2013). Degradation of FZD and LRP is abrogated upon treatment of cells with bafilomycin A1 but not with MG132, suggesting that degradation of the receptors occurs in the lysosome. Consistent with this, mutational analysis suggests that FZD4 is multi-monoubiquitinated (Mukai et al, 2010).
Identifier: R-HSA-3772435
Species: Homo sapiens
Compartment: cytosol
CSNK1E and DVL physically interact in vivo and CSNK1E phosphorylates DVL in response to WNT signaling (Peters et al, 1999; Sakanaka et al, 1999; Kishida et al, 2001; Gao et al, 2002; Hino et al, 2003; Klimowski et al, 2006; Bernatik et al, 2011). Phosphorylation by CSNK1E in the PDZ domain of DVL appears to be required for the recruitment of AXIN and the subsequent phosphorylation of LRP6 (Bernatik et al, 2011).
Identifier: R-HSA-4641205
Species: Homo sapiens
Compartment: plasma membrane
RSPO1-4 increase the levels of FZD and LRP6 receptors and decrease the amount of ZNRF3 at the plasma membrane. RSPO-induced internalization of ZNRF3 depends on LGR and the ubiquitin ligase activity of ZNRF3, and RSPO has been shown to bind directly to the extracellular region of ZNRF3 in an LGR-independent manner. These data are consistent with a model where RSPO promotes an interaction between ZNRF3 and LGR proteins that is required for downregulation of the ubiquitin ligase. In support of this model, artificial dimerization of ZNRF3 and LGR bypasses the requirement for RSPO in ZNRF3 internalization (Hao et al, 2012).
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