FZD1

Frizzled-1 is a protein that in humans is encoded by the FZD1 gene.

Function

Members of the 'frizzled' gene family encode 7-transmembrane domain proteins that are receptors for Wnt signaling proteins. The FZD1 protein contains a signal peptide, a cysteine-rich domain in the N-terminal extracellular region, 7 transmembrane domains, and a C-terminal PDZ domain-binding motif. The FZD1 transcript is expressed in various tissues.

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

FZD3

Frizzled-3 is a protein that in humans is encoded by the FZD3 gene.

Function

This gene is a member of the frizzled gene family. Members of this family encode seven-transmembrane domain proteins that are receptors for the Wingless type MMTV integration site family of signaling proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway. It may play a role in mammalian hair follicle development.

The function of this gene is largely derived from mouse studies. Fzd3 in the mouse functions through planar cell polarity signaling instead of the canonical Wnt/beta-catenin pathway. Fzd3 controls axon growth and guidance in the mouse nervous system, and migration of neural crest cells.

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External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

FZD7

Frizzled-7 is a protein that in humans is encoded by the FZD7 gene.

Members of the 'frizzled' gene family encode 7-transmembrane domain proteins that are receptors for Wnt signaling proteins. The FZD7 protein contains an N-terminal signal sequence, 10 cysteine residues typical of the cysteine-rich extracellular domain of Fz family members, 7 putative transmembrane domains, and an intracellular C-terminal tail with a PDZ domain-binding motif. FZD7 gene expression may downregulate APC function and enhance beta-catenin-mediated signals in poorly differentiated human esophageal carcinomas.

Interactions

FZD7 has been shown to interact with DLG4.

See also

References

External links

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.