| Description | Frizzleds are seven transmembrane-spanning proteins that constitute an unconventional class of G protein-coupled receptors [ ]. They have important regulatory roles during embryonic development [, ].Frizzleds expose their large N terminus on the extracellular side. The N-terminal, extracellular cysteine-rich domain (CRD) has been implicated as the Wnt binding domain and its structure has been solved [ ]. The cysteine-rich domain of Frizzled (Fz) is shared with other receptor tyrosine kinases that have roles in development including the muscle-specific receptor tyrosine kinase (MuSK), the neuronal specific kinase (NSK2), and ROR1 and ROR2. The cytoplasmic side of many Fz proteins has been shown to interact with the PDZ domains of PSD-95 family members and is thought to have a role in the assembly of signalling complexes. The conserved cytoplasmic motif of Fz, Lys-Thr-X-X-X-Trp, is required for activation of the beta-catenin pathway, and for membrane localisation and phosphorylation of Dsh.Three main signaling pathways are activated by agonist-activated Frizzled proteins: the Fz/beta-catenin pathway, the Fz/Ca2 pathway and the Fz/PCP (planar cell polarity) pathway [ ]. The Wnt/beta-catenin pathway is the best studied signalling pathway involving Fz receptors. In the Wnt/beta-catenin pathway the first downstream cytoplasmic components activated by Fz signalling include Dishevelled (Dsh) and/or its regulatory kinases.This entry represents the C-terminal transmembrane domain of Frizzled-4. Together with Frizzled-8, this protein has a major role in controlling ureteric growth in the developing kidney [ ]. In humans, mutations in the gene encoding Frizzled-4 are related to familial exudative vitreoretinopathy, a disorder characterized by the incomplete development of the retinal vasculature []. | Name | Frizzled-4, 7TM |
| Short Name | FZD4_7TM | Type | Domain |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
