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A Drosophila tissue polarity locus encodes a protein containing seven potential transmembrane domains

Nature volume 338, pages 263–264 (1989)Cite this article

Abstract

THE function of the frizzled (fz) locus in Drosophilia melanogaster is required to coordinate the cytoskeletons of epidermal cells to produce a parallel array of cuticular hairs and bristles (for example on the wild-type wing all hairs point towards the distal tip)1,2. In fz mutants it is not the structure of individual hairs and bristles that is altered, but their orientation with respect to their neighbours and the organism as a whole. Mitotic clone analysis3 indicates that fz has two functions in the developing wing. It is required for the proximal-distal transmission of an intercellular polarity signal, a process that is expected to be at least partly extracellular. It is also required for cells to respond to the polarity signal, which is expected to be a cytoplasmic function. The fz locus could encode either one bifunctional or two single-function proteins. We report here that, in pupae, fz produces a messenger RNA that encodes a protein with seven putative transmembrane domains. Thus, the Fz protein should contain both extracellular and cytoplasmic domains, which could function in the transmission and interpreta-tion of polarity information, respectively. This is the first reported sequence for the protein product of a tissue polarity gene.

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Author notes

  1. Charles R. Vinson

    Present address: Carnegie Institution of Washington, 115 West University Parkway, Baltimore, Maryland, USA

Authors and Affiliations

  1. Biology Department, Molecular Biology Institute,

    Charles R. Vinson, Sharon Conover & Paul N. Adler

  2. Cancer Center, Gilmer Hall, University of Virgina, Charlottesville, Virginia, 22901, USA

    Charles R. Vinson, Sharon Conover & Paul N. Adler

Authors
  1. Charles R. Vinson
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  2. Sharon Conover
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  3. Paul N. Adler
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Vinson, C., Conover, S. & Adler, P. A Drosophila tissue polarity locus encodes a protein containing seven potential transmembrane domains. Nature 338, 263–264 (1989). https://doi.org/10.1038/338263a0

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