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CD10/neutral endopeptidase 24.11 is phosphorylated by casein kinase II and
coassociates with other phosphoproteins including the lyn src- related
kinase
RK Ganju, RG Shpektor, DG Brenner and MA Shipp
Department of Medicine, Dana-Farber Cancer Institute, Harvard Medical
School, Boston, MA 02115, USA.
CD10/neutral endopeptidase 24.11 (NEP) regulates peptidemediated
proliferation of lymphoid progenitors and certain epithelial cells and is
itself regulated by cellular proliferation. To further characterize
mechanisms by which cell-surface signaling might regulate CD10/NEP
expression, we determined whether CD10/NEP was phosphorylated and whether
the enzyme co-associated with additional cellular phosphoproteins. The
CD10/NEP cytoplasmic tall contains two consensus recognition sequences for
casein kinase II (CKII), a serine and threonine kinase that increases in
activity following peptide signaling. In standard in vitro kinase assays,
CKII phosphorylated full- length recombinant CD10/NEP but did not
phosphorylate a truncated CD10/NEP protein that lacked the transmembrane
region and cytoplasmic tail. To determine whether CD10/NEP might interact
with additional cellular phosphoproteins, in vitro kinase assays were
performed on CD10/NEP immune complexes from Nalm-6 cells. Three additional
tyrosine phosphoproteins of approximately 40 kD, approximately 58 kD, and
approximately 75 kD were identified in the CD10/NEP immunoprecipitates. The
approximately 56-kD CD10/NEP-associated phosphoprotein was
immunoprecipitated with an anti-lyn antibody confirming its identity as the
lyn src-related kinase. Taken together, these data indicate that CD10/NEP
is itself phosphorylated by CKII and that CD10/NEP co- associates with
additional tyrosine phosphoproteins including lyn.
Volume 88,
Issue 11,
pp. 4159-4165,
12/01/1996
Copyright © 1996 by The American Society of Hematology
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