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J Biol Chem, Vol. 273, Issue 19, 11660-11666, May 8, 1998
From the Burnham Institute, La Jolla, California 92037
BAG-1 is a regulator of heat shock protein (Hsp)
70/Hsc70 family proteins that interacts with steroid hormone receptors.
The recently identified BAG-1 long (BAG-1L) protein, an isoform of BAG-1 that arises from translation initiation at a noncanonical CUG
codon, was co-immunoprecipitated with androgen receptors (AR) from
LNCaP prostate cancer cells and other cell lysates, whereas the shorter
originally identified BAG-1 and BAG-1M (RAP 46) proteins were not.
BAG-1L, but not BAG-1 or BAG-1M (RAP46), also markedly enhanced the
ability of AR to transactivate reporter gene plasmids containing an
androgen response element (ARE) in PC3 prostate cancer and other cell
lines. A C-terminal region deletion mutant of BAG-1L failed to
co-immunoprecipitate with AR and functioned as a trans-dominant
inhibitor of BAG-1L, impairing AR-induced transactivation of
ARE-containing reporter plasmids. In addition, BAG-1L significantly
reduced the concentrations of 5
BAG-1L Protein Enhances Androgen Receptor Function
-dihydrotestosterone (DHT) required
for AR activity but did not induce ligand-independent transactivation.
BAG-1L also markedly improved the ability of AR to transactivate
reporter genes when cells were cultured with DHT in combination with
the anti-androgen cyproterone acetate. The effects of BAG-1L on AR
could not be explained by detectable alterations in the DHT-induced
translocation of AR from cytosol to nucleus, nor by BAG-1L-induced
increases in the amounts of AR protein. These findings implicate BAG-1L
in the regulation of AR function and may have relevance to mechanisms
of prostate cancer resistance to hormone-ablative and anti-androgen
therapy.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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