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J Biol Chem, Vol. 275, Issue 3, 1565-1569, January 21, 2000
o Subunits via
the Proteosome Pathway Is Induced by the hsp90-specific
Compound Geldanamycin*
¶,
From the § Renal Division, Department of Medicine,
Brigham and Women's Hospital and Harvard Medical School, Boston,
Massachusetts 02115 and Fundación Investigaciones
Biológicas Aplicadas, Vieytes 3103, 7600 Mar del Plata, Argentina
One mechanism utilized by cells to maintain
signaling pathways is to regulate the levels of specific signal
transduction proteins. The compound geldanamycin (GA) specifically
interacts with heat shock protein 90 (hsp90) complexes and has been
widely utilized to study the role of hsp90 in modulating the function
of signaling proteins. In this study, we used GA to demonstrate that
levels of heterotrimeric G
subunits can be regulated through
interactions with hsp90. In a dose-dependent manner, GA
significantly reduced the steady state levels of endogenous
Go expression in two cell lines (PC12 and GH3) and
had a similar effect on Go transiently expressed in COS
cells. Go synthesis and degradation was studied in PC12
cells and in transiently transfected COS cells. 35S
labeling followed by immunoprecipitation demonstrated no effect of GA
on the rate of Go synthesis, but GA accelerated
degradation of Go in both PC12 cells and COS cells. The
use of inhibitors, including lactacystin (a proteosome-specific
inhibitor), suggests that Go is predominantly degraded
through the proteosome pathway. In vitro translated
35S-labeled Go could be detected in hsp90
immunoprecipitates, and this interaction did not require N-terminal
myristoylation. Taken together, these results suggest that
heterotrimeric Go subunits are protected from
degradation by interaction with hsp90 and that the interaction of G
subunits with heat shock proteins may be a general mechanism for
regulating G levels in the cell.
Career Investigator of the Consejo Nacional de Investigaciones
Cientìficas y Tecnológicas, Argentina.
¶
To whom correspondence should be addressed: FIBA
(Fundación para Investigaciones Biológicas
Aplicadas)-INBIOP, Vieytes 3103, 7600 Mar del Plata, Argentina. Tel.:
54-223-474-8784; Fax: 54-223-475-7120; E-mail:
lbusconi@hotmail.com.
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