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(Received for publication, November 1, 1995) 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.
Volume 271,
Number 8,
Issue of February 23, 1996 pp. 4468-4476
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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