Abstract: |
Activins are cytokines of the transforming growth factor β superfamily that control various events during vertebrate embryo development and cell differentiation in the adult, and act through transmembrane receptors that contain a cytoplasmic protein-serine/threonine kinase domain. We describe the identification, deduced primary structure, and expression pattern of Atr-II, a receptor serine/threonine kinase found in Drosophila. With the exception of the spacing of 10 cysteine residues, the extracellular domain of Atr-II is very dissimilar from those of vertebrate activin receptors, yet it binds activin with high affinity and specificity. The kinase domain sequence of Atr-II is 60% identical to those of activin receptors from vertebrates, suggesting similarities in their signaling mechanisms. Maternal Atr-II transcript and its product are abundant in the oocyte. During development, the highest levels of Atr-II transcript and protein are observed in the mesoderm and gut. The possible role of an activin signaling system in Drosophila development is discussed. |
Keywords: |
signal transduction; nonhuman; comparative study; mouse; animal; gene expression; embryo; drosophila; embryo development; vertebrata; rna; in situ hybridization; molecular cloning; cloning, molecular; amino acid sequence; molecular sequence data; sequence homology, amino acid; rna, messenger; sequence alignment; protein-serine-threonine kinases; drosophila melanogaster; receptor affinity; receptor binding; complementary dna; dna, complementary; receptors, growth factor; cell receptor; activin; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; activin receptors; threonine kinase; genes, structural, insect; protein-serine; receptor kinase; transforming growth factor β superfamily
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