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J Biol Chem, Vol. 273, Issue 18, 11173-11176, May 1, 1998
From the Hematology Division, Brigham and Women's Hospital,
Harvard Medical School, Boston, Massachusetts 02115
Erythropoietin (Epo) is believed to transduce a
signal by bringing two Epo receptors into close proximity, enabling
cross-phosphorylation. We compared monomeric Epos with homodimers in
which two Epo monomers are linked by polyglycine. Monomeric Epo mutant
R103A is unable to support Epo-dependent cell growth or
trigger Janus kinase 2 and STAT5 activation, even at
concentrations greater than 7,000 times that sufficient for
wild-type Epo activity. In contrast, R103A homodimer induces
proliferation and transduces signal at concentrations similar to that
of wild-type Epo monomer and homodimer. These experiments show that two
discrete domains on Epo are required for receptor binding and
activation. Our results also suggest that the EpoR can be dimerized by
different forms and sizes of molecules, as long as two
recognition motifs are provided in the same molecule. Design of
other dimeric molecules may enhance our understanding of
cytokine specificity and signal transduction.
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