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摘要
En 中文
The recent discovery of estrogen receptor β as a biological partner
with estrogen receptor β in mediating the estrogen response has come
at precisely the same time as intensive research is revealing the role played
by downstream coregulator proteins in linking nuclear hormone receptor
activity to general transcription machinery involved in gene transcriptional
activation. In what is a rapidly evolving area of research, findings to date
have led to a proposed model of hormonal action, in which a receptor activated
by estrogen or cell-membrane-derived phosphorylation-dependent signaling
pathways promotes recruitment of selected members of the multifunctional
steroid receptor coactivator family and the cointegrators, p300/CBP and
P/CAF. The intrinsic histone acetylase activity mediated by these
coactivator and cointegrator proteins, alters chromatin structure giving rise
to increased transcriptional efficiency. On the other hand, antiestrogen-bound
receptors favour the assembly of receptor-corepressor complexes containing the
sequence-related corepressors N-CoR (nuclear receptor corepressor) or SMRT
(silencing mediator of retinoid and thyroid hormone receptors), localizing
histone deacetylase activity to the promoter and leading to transcriptional
repression. The model predicts that a change in the balance between
corepressor and coactivator expression in favour of coactivators, might result
in antiestrogen resistance. Together with available crystal structure data for
estrogen- and antiestrogen-bound receptors, these studies have provided
valuable insights into events that occur subsequent to receptor interaction
with specific DNA sequences and have helped define the molecular basis of
estrogen and antiestrogen activity.
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