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Extracellular domain of the boss transmembrane ligand acts as an antagonist of the sev receptor

Nature volume 361, pages 732–736 (1993)Cite this article

Abstract

THE fate of the R7 photoreceptor cell in the Drosophila compound eye is established by a specific inductive interaction between the R8 photoreceptor neuron and the R7 precursor cell1. This induction is mediated by two cell-surface proteins: the ligand, bride of sevenless2 (boss), and sevenless (sev), a tyrosine-kinase receptor3–5. The structure of boss is unique for a ligand of a tyrosine-kinase receptor. It contains a large extracellular domain, seven transmembrane segments, and a carboxy-terminal cytoplasmic tail6,7. Here we report that: (1) boss activates tyrosine phosphorylation of the sev receptor; (2) the seven transmembrane domain of boss is necessary for its function; and (3) a soluble form of boss acts as an antagonist of the sev receptor both in vivo and in vitro.

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Author notes

  1. A. C. Hart

    Present address: Department of Molecular Biology, Wellman 8, Massachusetts General Hospital, Boston, Massachusetts, 02114, USA

  2. H. Krämer

    Present address: Department of Cell Biology and Neuroscience, University of Texas, Southwestern Medical Center, Dallas, Texas, 75235, USA

Authors and Affiliations

  1. Howard Hughes Medical Institute, Department of Biological Chemistry, The Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California, 90024, USA

    A. C. Hart, H. Krämer & S. L. Zipursky

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  1. A. C. Hart
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  2. H. Krämer
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  3. S. L. Zipursky
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Hart, A., Krämer, H. & Zipursky, S. Extracellular domain of the boss transmembrane ligand acts as an antagonist of the sev receptor. Nature 361, 732–736 (1993). https://doi.org/10.1038/361732a0

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