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Ligand-dependent polyubiquitination of c-kit gene product: a possible
mechanism of receptor down modulation in M07e cells
K Miyazawa, K Toyama, A Gotoh, PC Hendrie, C Mantel and HE Broxmeyer
First Department of Internal Medicine (Hematology/Oncology), Tokyo Medical
College, Japan.
Quantities of proteins in cells are balanced by protein synthesis and
degradation. Protein ubiquitination is an important adenosine- triphosphate
dependent proteolytic pathway for "short-lived" proteins. We show that
soluble steel-factor (SLF) stimulation at 37 degrees C rapidly induced
polyubiquitination of c-kit protein in growth-factor- dependent
human-myeloid cell line M07e, resulting in smeared, retarded migration of
c-kit protein in sodium dodecyl sulfate-polyacrylamide gel electrophoresis
in the molecular weight region of 145 kD. Receptor ubiquitination was
almost completely absent when cells were treated with SLF at 4 degrees C or
at 37 degrees C in the presence of 0.2% sodium azide, or when the cells
were pretreated with anti-c-kit monoclonal antibody or genistein, a
tyrosine-kinase inhibitor. This suggested that c-kit ubiquitination was
ligand dependent and appeared to require intrinsic tyrosine-kinase
activation of the c-kit protein. Flow-cytometric analysis of c-kit
expression on the cell surface of M07e cells showed down modulation of
c-kit within 5 minutes after soluble-SLF treatment at 37 degrees C.
However, rapid receptor down modulation was almost completely suppressed
when cells were treated with SLF at 4 degrees C or at 37 degrees C in the
presence of 0.2% sodium azide, conditions that concomitantly suppressed
polyubiquitination of c-kit protein. In addition, these conditions almost
completely suppressed radiolabeled SLF (125I-SLF) internalization after
ligand-receptor interaction. Pulse-chase studies of 35S-methionine-labeled
c-kit protein showed that SLF stimulation at 37 degrees C strikingly
enhanced c-kit degradation (T1/2; approximately 20 minutes) compared with
that in cells stimulated with SLF at 4 degrees C or at 37 degrees C with
0.2% sodium azide. However, in the presence of chloroquine, which blocks
lysosomal degradation, this ligand-induced c-kit degradation at 37 degrees
C was only suppressed in part. These data suggest that SLF-induced
polyubiquitination of the c- kit receptor protein may play a role in
regulation of c-kit-encoded protein-receptor expression in M07e cells.
Volume 83,
Issue 1,
pp. 137-145,
01/01/1994
Copyright © 1994 by The American Society of Hematology
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