Matches in Nanopublications for { <http://www.tkuhn.ch/bel2nanopub/RAC3-8pgxtnQGkr6_F0deClc3jQGqdjD-Th8H1XpsCtJ8#_7> ?p ?o ?g. }
Showing items 1 to 2 of
2
with 100 items per page.
- _7 value "In this study, we show that a p160 coactivator contributes to the ligand- independent ER activation of a target gene in a cellular model in which ER, coactivator, and target gene are endogenous. Using transfected cells, we further show that the full-length ER can interact physically and functionally with all three p160/SRCs and CBP in the absence of ligand in vivo and that mutation of Ser104/106/118 to Ala residues in ER affects these interactions. In addition, mutation of these residues affects ER coactivation by a subset of coactivators in the presence of E2, albeit to a lesser extent than in the absence of hormone. Further analysis reveals that mutations of both Ser104/106 and Ser118 decrease ligand-independent SRC-1 coactivation of ER activity by two mechanisms. First, there is a seemingly indirect effect on SRC-1 recruitment that, surprisingly, requires other receptor domains in addition to A/B, which is consistent with our finding that SRC-1 enhancement of the ligand- independent interaction between the A/B and DEF regions is regulated by the Ser104/106/118 phosphorylation sites. Secondly, we observe an effect on SRC-1 coactivation of the A/B domain that does not depend on the remainder of the molecule. further show that the full-length ER can interact physically and functionally with all three p160/SRCs and CBP in the absence of ligand in vivo" provenance.
- _7 wasQuotedFrom 12714702 provenance.