Abstract
The cytoplasmic domains of the erythropoietin receptor essential for signal transduction were identified by assessing a series of truncated and deletional mutant receptors. A 91-amino acid region proximal to the transmembrane domain was required for growth signaling. In this region, residues between 353Pro and 362His and between 278Gln and 308Leu appeared to constitute the essential cytoplasmic domains. These two domains contain the conserved amino acids common in the cytokine receptor superfamily, which indicates that these domains in the cytoplasmic regions of the erythropoietin receptor may be important for interaction with common signal transducers or protein tyrosine kinases.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cell Division / drug effects
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Cytoplasm / metabolism
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Dose-Response Relationship, Drug
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Erythropoietin / metabolism
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Erythropoietin / pharmacology*
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Humans
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Interleukin-3 / pharmacology
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Kinetics
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Mice
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Molecular Sequence Data
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Mutagenesis, Site-Directed*
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Oligodeoxyribonucleotides
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Receptors, Cell Surface / genetics
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Receptors, Cell Surface / metabolism*
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Receptors, Erythropoietin
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Recombinant Proteins / metabolism
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Recombinant Proteins / pharmacology
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Transfection
Substances
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Interleukin-3
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Oligodeoxyribonucleotides
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Receptors, Cell Surface
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Receptors, Erythropoietin
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Recombinant Proteins
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Erythropoietin