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Laboratory of Receptor Biology and Gene Expression (C.T.B., R.W.,
J.C.R., C.L., G.L.H.) National Cancer Institute National
Institutes of Health Bethesda, Maryland 20892-5055
Molecular Regulation & Neuroendocrinology Section (P.M.,
P.M.Y.) Clinical Endocrinology Branch National Institute of
Diabetes, Digestive and Kidney Diseases National Institutes of
Health Bethesda, Maryland 20892
Department of Pathology
(H.M., M.R.S.) University of Southern California Los Angeles,
California 90033
The glucocorticoid receptor interacting protein-1
(GRIP1) is a member of the steroid receptor coactivator (SRC) family of
transcriptional regulators. Green fluorescent protein (GFP) fusions
were made to full-length GRIP1, and a series of GRIP1 mutants lacking
the defined regulatory regions and the intracellular distribution of
these proteins was studied in HeLa cells. The distribution of GRIP1 was
complex, ranging from diffuse nucleoplasmic to discrete intranuclear
foci. Formation of these foci was dependent on the C-terminal region of
GRIP1, which contains the two characterized transcriptional activation
domains, AD1 and AD2. A subpopulation of GRIP1 foci associate with
ND10s, small nuclear bodies that contain several proteins including
PML, SP100, DAXX, and CREB-binding protein (CBP). Association with the
ND10s is dependent on the AD1 of GRIP1, a region of the protein
previously described as a CBP-interacting domain. The GRIP1 foci are
enriched in components of the 26S proteasome, including the core 20S
proteasome, PA28
, and ubiquitin. In addition, the irreversible
proteasome inhibitor lactacystin induced an increase in the total
fluorescence intensity of the GFP-GRIP1 expressing cells, demonstrating
that GRIP1 is degraded by the proteasome. These findings suggest the
intriguing possibility that degradation of GRIP1 by the 26S proteasome
may be a key component of its regulation.
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