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J. Biol. Chem., Vol. 265, Issue 29, 17456-17462, 10, 1990
Y Murayama, T Okamoto, E Ogata, T Asano, T Iiri, T Katada, M Ui, JH Grubb, WS Sly and I Nishimoto
The rat insulin-like growth factor II (IGF-II) receptor develops
transmembrane signaling functions by directly coupling to a guanine
nucleotide-binding protein (G protein) having a 40-kDa alpha subunit, Gi-2,
whereas recent studies have indicated that the IGF-II receptor is a
molecule identical to the cation-independent mannose 6-phosphate receptor
(CI-MPR), a receptor implicated in lysosomal enzyme sorting. In this study,
by using vesicles reconstituted with the clonal human CI- MPR and G
proteins, we indicated that the CI-MPR could stimulate guanosine
5'-O-(3-thiotriphosphate) (GTP gamma S) binding and GTPase activities of Gi
proteins in response to IGF-II. The stimulatory effect of IGF-II on Gi-2
depended on the reconstituted amount of the CI-MPR; it could not be found
in vesicles reconstituted with Gi-2 alone; and it was also observed on Gi-1
reconstituted with the CI-MPR in phospholipid vesicles. Of interest, such
stimulatory effect was not reproduced by Man-6-P in CI-MPR vesicles
reconstituted with either G protein. Furthermore, the affinity for
Man-6-P-mediated beta-glucuronidase binding to several kinds of native cell
membranes was not reduced by 100 microM GTP gamma S. Instead, however,
Man-6-P dose-dependently inhibited IGF-II-induced Gi-2 activation with an
IC50 of 6 microM in vesicles reconstituted with the CI-MPR and Gi-2. The
action of 100 nM IGF-II was completely abolished by 1 mM Man-6-P. Such an
inhibitory effect of Man-6-P was reproduced by 4000 times lower
concentrations of beta-glucuronidase or similar concentrations of fructose
1-phosphate, but not by mannose or glucose 6-phosphate. These results
indicate that the human CI-MPR has two distinct signaling functions that
positively or negatively regulate the activity of Gi-2 in response to the
binding of IGF-II or Man-6-P.
Distinctive regulation of the functional linkage between the human cation-independent mannose 6-phosphate receptor and GTP-binding proteins by insulin-like growth factor II and mannose 6-phosphate
Fourth Department of Internal Medicine, University of Tokyo School of Medicine, Japan.
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