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Association of the p85 regulatory subunit of phosphatidylinositol 3- kinase
with an essential erythropoietin receptor subdomain
TC He, H Zhuang, N Jiang, MD Waterfield and DM Wojchowski
Department of Molecular and Cell Biology, Pennsylvania State University,
University Park 16802.
Using an active, HAI epitope-tagged form of the murine erythropoietin (EPO)
receptor and via direct coimmunoprecipitation, the p85 regulatory subunit
of phosphatidyl inositol-3 kinase (p85/PI3-K) is shown to associate with
the EPO receptor in transfected FDC-P1 cell lines. Coimmunoprecipitation of
p85 with epitope-tagged EPO receptors was observed initially in FDC-HER
cells labeled metabolically with [32P]orthophosphate, and association of
these factors was confirmed by Western analyses of receptor
immunoprecipitates using p85 antiserum. Interestingly, this association
occurred in the absence of ligand, and exposure of FDC-HER cells to EPO did
not detectably affect levels of receptor-associated p85 or overall levels
of p85 phosphorylation. However, EPO was observed to stimulated the rapid
formation of phosphatidylinositol 32P-phosphate in FDC-HER and FDC-ER
cells. Through baculovirus-mediated expression of epitope-tagged EPO
receptor forms in SF9 cells, domains for p85 association were mapped.
Analyses of receptor forms with cytosolic truncations and deletions
delineated a candidate subdomain for p85 binding to an essential extended
box-2 region (P329-E374; including a putative motif for SH2 binding,
Y343LVL). These findings extend a mechanistic alignment between the EPO
receptor and protein tyrosine kinase-encoding receptors that likewise
activate PI3-K, and expand the importance of further defining pathways to
PI3-K activation.
Volume 82,
Issue 12,
pp. 3530-3538,
12/15/1993
Copyright © 1993 by The American Society of Hematology
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