Identification, characterization, and developmental regulation of a receptor guanylyl cyclase expressed during early stages of Drosophila development

L. McNeil, M. Chinkers, M. Forte

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

Membrane forms of guanylyl cyclase are single-transmembrane proteins that are activated by the binding of specific peptide ligands to their extracellular domains. In this report, we describe the identification and characterization of a Drosophila cDNA clone encoding a protein, DrGC-1, with high sequence identity to members of this family of receptor proteins. The protein contains a single, hydrophobic domain predicted to represent a transmembrane segment separating an extracellular domain with significant sequence identity (30%) to sea urchin egg peptide receptors from intracellular domains containing a protein kinase-like domain followed by a region with high sequence identity (65%) to cyclase catalytic domains found in receptor guanylyl cyclases from both vertebrates and invertebrates. In contrast to other members of this family, DrGC-1 is predicted to contain a carboxyl-terminal extension of 430 residues that has no homology to any described protein. Northern analysis indicates that DrGC-1 transcripts are present at variable levels in all stages of development. In situ hybridization demonstrates that high levels of uniformly distributed transcript are present in 0-2-h embryos. Later in embryogenesis (14-18 h), elevated levels of hybridization appear to be preferentially associated with muscle fibers.

Original languageEnglish (US)
Pages (from-to)7189-7196
Number of pages8
JournalJournal of Biological Chemistry
Volume270
Issue number13
DOIs
StatePublished - Jan 1 1995

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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