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• W2891566522 endingPage "17887" @default.
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• W2891566522 abstract "The Frizzled (FZD) proteins belong to class F of G protein–coupled receptors (GPCRs) and are essential for various pathways involving the secreted lipoglycoproteins of the wingless/int-1 (WNT) family. A WNT-binding cysteine-rich domain (CRD) in FZDs is N-terminally located and connected to the seven transmembrane domain–spanning receptor core by a linker domain that has a variable length in different FZD homologs. However, the function and importance of this linker domain are poorly understood. Here we used systematic mutagenesis of FZD6 to define the minimal N-terminal domain sufficient for receptor surface expression and recruitment of the intracellular scaffold protein Dishevelled (DVL). Further, we identified a triad of evolutionarily conserved cysteines in the FZD linker domain that is crucial for receptor membrane expression and recruitment of DVL. Our results are in agreement with the concept that the conserved cysteines in the linker domain of FZDs assist with the formation of a common secondary structure in this region. We propose that this structure could be involved in agonist binding and receptor activation mechanisms that are similar to the binding and activation mechanisms known for other GPCRs. The Frizzled (FZD) proteins belong to class F of G protein–coupled receptors (GPCRs) and are essential for various pathways involving the secreted lipoglycoproteins of the wingless/int-1 (WNT) family. A WNT-binding cysteine-rich domain (CRD) in FZDs is N-terminally located and connected to the seven transmembrane domain–spanning receptor core by a linker domain that has a variable length in different FZD homologs. However, the function and importance of this linker domain are poorly understood. Here we used systematic mutagenesis of FZD6 to define the minimal N-terminal domain sufficient for receptor surface expression and recruitment of the intracellular scaffold protein Dishevelled (DVL). Further, we identified a triad of evolutionarily conserved cysteines in the FZD linker domain that is crucial for receptor membrane expression and recruitment of DVL. Our results are in agreement with the concept that the conserved cysteines in the linker domain of FZDs assist with the formation of a common secondary structure in this region. We propose that this structure could be involved in agonist binding and receptor activation mechanisms that are similar to the binding and activation mechanisms known for other GPCRs." @default.
• W2891566522 created "2018-09-27" @default.
• W2891566522 creator A5006646972 @default.
• W2891566522 creator A5008208466 @default.
• W2891566522 creator A5060927839 @default.
• W2891566522 creator A5073010585 @default.
• W2891566522 date "2018-11-01" @default.
• W2891566522 modified "2023-10-15" @default.
• W2891566522 title "Functional dissection of the N-terminal extracellular domains of Frizzled 6 reveals their roles for receptor localization and Dishevelled recruitment" @default.
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• W2891566522 doi "https://doi.org/10.1074/jbc.ra118.004763" @default.
• W2891566522 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6240854" @default.
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• W2891566522 hasPublicationYear "2018" @default.
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