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ZFIN ID: ZDB-PUB-961101-17
A large family of putative transmembrane receptors homologous to the product of the Drosophila tissue polarity gene frizzled
Wang, Y., Macke, J.P., Abella, B.S., Andreasson, K., Worley, P., Gilbert, D.J., Copeland, N.G., Jenkins, N.A., and Nathans, J.
Date: 1996
Source: The Journal of biological chemistry 271(8): 4468-4476 (Journal)
Registered Authors: Wang, Yihong
Keywords: none
MeSH Terms:
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Caenorhabditis elegans
  • Central Nervous System/embryology
  • Central Nervous System/growth & development
  • Central Nervous System/metabolism
  • Chickens
  • Chromosome Mapping
  • Cloning, Molecular
  • DNA Primers
  • DNA, Complementary
  • Drosophila Proteins*
  • Drosophila melanogaster/genetics
  • Drosophila melanogaster/metabolism*
  • Embryonic and Fetal Development
  • Exons
  • Frizzled Receptors
  • Genes, Insect*
  • Humans
  • In Situ Hybridization
  • Insect Hormones/biosynthesis
  • Insect Hormones/chemistry*
  • Introns
  • Mammals
  • Membrane Proteins/biosynthesis
  • Membrane Proteins/chemistry*
  • Membrane Proteins/genetics*
  • Mice
  • Molecular Sequence Data
  • Multigene Family*
  • Nematoda/metabolism
  • Polymerase Chain Reaction
  • Protein Structure, Secondary
  • Rats
  • Receptors, Cell Surface/biosynthesis
  • Receptors, Cell Surface/chemistry*
  • Receptors, G-Protein-Coupled/biosynthesis
  • Receptors, G-Protein-Coupled/chemistry
  • Sea Urchins
  • Sequence Homology, Amino Acid
  • Zebrafish
PubMed: 8626800 Full text @ J. Biol. Chem.
In Drosophila melanogaster, the frizzled gene plays an essential role in the development of tissue polarity as assessed by the orientation of cuticular structures. Through a combination of random cDNA sequencing, degenerate polymerase chain reaction amplification, and low stringency hybridization we have identified six novel frizzled homologues from mammals, at least 11 from zebrafish, several from chicken and sea urchin, and one from Caenorhabditis elegans. The complete deduced amino acid sequences of the mammalian and nematode homologues share with the Drosophila frizzled protein a conserved amino-terminal cysteine-rich domain and seven putative transmembrane segments. Each of the mammalian homologues is expressed in a distinctive set of tissues in the adult, and at least three are expressed during embryogenesis. As hypothesized for the Drosophila frizzled protein, the frizzled homologues are likely to act as transmembrane receptors for as yet unidentified ligands. These observations predict the existence of a family of signal transduction pathways that are homologous to the pathway that determines tissue polarity in Drosophila.