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J Biol Chem, Vol. 273, Issue 18, 11183-11188, May 1, 1998
From the First Department of Medicine, Toyama Medical and
Pharmaceutical University, 2630 Sugitani, Toyama 930-01, Japan
We previously reported three families with type A
insulin-resistant syndrome who had mutations, either
Asp1179 or Leu1193, in the kinase domain
of the insulin receptor. The extreme insulin resistance of these
patients was found to be caused by the decreased number of insulin
receptors on the cell surface, due to the intracellular rapid
degradation (Imamura, T., Takata, Y., Sasaoka, T., Takada, Y., Morioka,
H., Haruta, T., Sawa, T., Iwanishi, M., Yang, G. H., Suzuki, Y.,
Hamada, J., and Kobayashi, M. (1994) J. Biol. Chem.
269, 31019-31027). In the present study, we first examined whether
these mutations caused rapid degradation of unprocessed proreceptors,
using the exon 13 deleted mutant insulin receptors (
Ex13-IR), which
were accumulated in the endoplasmic reticulum as unprocessed
proreceptors. The addition of Asp1179 or
Leu1193 mutation to Ex13-IR caused accelerated
degradation of the unprocessed Ex13-IR in the transfected COS-7
cells. Next, we tested whether these mutant receptors were degraded by
the proteasome. Treatment with proteasome inhibitors Z-Leu-Leu-Nva-H
(MG-115) or Z-Leu-Leu-Leu-H (MG-132) prevented the accelerated
degradation of these mutant receptors, resulting in increased amounts
of the mutant receptors in the COS-7 cells. Essentially the same
results were obtained in the patient's transformed lymphocytes.
Finally, we found that these mutant receptors bound to heat shock
protein 90 (Hsp90). To determine whether Hsp90 played an important role
in the accelerated receptor degradation, we examined the effect of
anti-Hsp90 antibody on the mutant receptor degradation. The
microinjection of anti-Hsp90 antibody into cells prevented the
accelerated degradation of both Asp1179 and
Leu1193 mutant insulin receptors. Taken together, these
results suggest that Hsp90 is involved in dislocation of the mutant
insulin receptors out of the endoplasmic reticulum into the cytosol,
where the mutant receptors are degraded by the proteasome.
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