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Roles of the N and C terminal domains of the interleukin-3 receptor alpha
chain in receptor function
SC Barry, E Korpelainen, Q Sun, FC Stomski, PA Moretti, H Wakao, RJ D'Andrea, MA Vadas, AF Lopez and GJ Goodall
Hanson Centre for Cancer Research, Adelaide, Australia.
The interleukin-3 (IL-3), granulocyte-macrophage colony-stimulating factor,
and IL-5 receptor alpha chains are each composed of three extracellular
domains, a transmembrane domain and a short intracellular region. Domains 2
and 3 constitute the cytokine receptor module (CRM), typical of the
cytokine receptor superfamily; however, the function of the N-terminal
domain is not known. We have investigated the functions of the N-terminal
and C-terminal domains of the IL-3 receptor (IL-3R) alpha chain. We find
that cells transfected with the receptor beta chain (h beta c) and a
truncated IL-3R alpha that is devoid of the intracellular region fail to
proliferate or to activate STAT5 in response to human IL-3, despite binding
the IL-3 with affinity indistinguishable from that of full-length receptor.
In addition, IL-3- induced phosphorylation of h beta c was not detected.
Thus, the IL-3R alpha intracellular region does not contribute detectably
to stabilization of the receptor/ligand complex, but is essential for
signal propagation. In contrast, a truncated IL-3R alpha with the N-
terminal domain deleted interacts functionally with the beta chain; mouse
cells transfected with these receptor chains proliferate in response to
human IL-3 and STAT5 transcription factor is activated. High- and
low-affinity binding sites are retained, although the affinity for IL-3 is
decreased 15-fold, indicating a significant role for the N-terminal domain
in IL-3 binding.
Volume 89,
Issue 3,
pp. 842-852,
02/01/1997
Copyright © 1997 by The American Society of Hematology
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