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(Received for publication, April 14, 1997)
From the Two leucines (Leu986 and
Leu987) have recently been shown to take part in the
control of human insulin receptor (HIR) internalization (Renfrew-Haft,
C., Klausner, R. D., and Taylor, S. I. (1994) J. Biol. Chem. 269, 26286-26294). The aim of the present study was to further investigate the exact mechanism of this control process. Constitutive and insulin-induced HIR internalizations were studied biochemically and morphologically in NIH 3T3 cells overexpressing either a double alanine (amino acid residues 986-987) mutant HIR (HIR
AA1) or HIR truncated at either amino acid residue 981 (HIR These results indicate that the dileucine motif is not sufficient by
itself, but participates in anchoring HIR on microvilli and that
another sequence, located downstream from position 1000 is crucial for
this event. This dileucine motif also plays a role in HIR segregation
in clathrin-coated pits. This latter function is additive with that of
the tyrosine-based motifs but the role of the dileucine motif
predominates. Eventually, the clathrin-coated pit anchoring function of
the dileucine motif is independent of receptor kinase activation in
contrast to the tyrosine-based motifs.
Volume 272, Number 35,
Issue of August 29, 1997
pp. 21685-21691
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
Department of Morphology, University of
Geneva, 1211 Geneva, Switzerland and the § Diabetes
Branch, NIDDK, National Institutes of Health,
Bethesda, Maryland 20892
981) or
1000 (HIR 1000). Data collected indicate that: (a) the three mutant HIR show a reduced association with microvilli as compared
with HIR wild-type; (b) the two receptors containing the
dileucine motif (HIR WT and HIR 1000) show the highest propensity to
associate with clathrin-coated pits, independently of kinase activation; (c) the two receptors lacking the dileucine
motif but containing two tyrosine-based motifs, previously described as
participating in clathrin-coated pit segregation, associate with these
surface domains with a lower affinity than the two others,
(d) in the presence of the kinase domain, an unmasking of
the tyrosine-based motifs mediated by kinase activation is required.
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