Linked Life Data

20734429

Source:http://linkedlifedata.com/resource/pubmed/id/20734429

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2010-9-30
pubmed:abstractText
Four and a half LIM domain protein 2 (FHL2) has been implicated in development and progression of various types of cancers. However, little is known about the biological function of FHL2 in breast cancer. Here, we report that FHL2 physically and functionally interacts with estrogen receptors (ER? and ER?), important regulators of breast cancer development and progression. The N-terminal half LIM domain or a single LIM domain of FHL2 was sufficient for its interaction with ER? and ER?. Overexpression of FHL2 reduced ER transcriptional activity in breast cancer cells, whereas reduction of endogenous FHL2 with FHL2 small interfering RNA enhanced ER transactivation. Moreover, FHL2 cooperates with Smad4, a previously known corepressor for ER?, to inhibit ER? transcriptional activity as well as expression of the estrogen-responsive gene cathepsin D. The synergistic inhibition of ER? transcriptional activity by FHL2 and Smad4 may be due to enhanced interaction of Smad4 with ER? by FHL2, because FHL2(1-156), the FHL2 deletion mutant, which showed no synergistic effect, failed to increase such interaction. These data suggested the cooperative regulation of estrogen signaling by FHL2 and Smad4 in breast cancer cells, and might provide a new regulation mechanism underlying breast cancer development and progression.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1521-6551
pubmed:author
pubmed:copyrightInfo
© 2010 IUBMB IUBMB Life.
pubmed:issnType
Electronic
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
669-76
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Synergistic repression of estrogen receptor transcriptional activity by FHL2 and Smad4 in breast cancer cells.
pubmed:affiliation
Department of Medical Molecular Biology, Beijing Institute of Biotechnology, Beijing 100850, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't