Linked Life Data

8226975

Source:http://linkedlifedata.com/resource/pubmed/id/8226975

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
1993-12-13
pubmed:abstractText
Transcriptional regulation by thyroid hormone is mediated through its nuclear receptors, which bind to target response elements as homodimers or as heterodimers with proteins such as retinoid X receptors (RXR). Thyroid hormone response elements exhibit remarkable flexibility in that the receptor binding half-sites can be arranged as direct repeats, inverted repeats, or everted repeats. We report that a limited region at the carboxyl-terminal end of the thyroid hormone receptor differentially contributes to the formation of receptor homo- and heterodimers. The functionally inactive thyroid hormone receptor splicing variant alpha 2, which is altered at the juncture of the homo- and heterodimerization domains, cannot form homodimers. However, alpha 2 can form a heterodimer when bound to half-sites arranged as a direct repeat spaced by 4 base pairs (DR4), but not with other arrangements of response element half-sites. The alpha 2-RXR heterodimer strongly inhibits wild type receptor function mediated by the DR4 element, suggesting that the alpha 2 isoform modulates thyroid hormone action by binding as an antagonist to a subset of response elements.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24278-82
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Distinct dimerization domains provide antagonist pathways for thyroid hormone receptor action.
pubmed:affiliation
Thyroid Unit, Massachusetts General Hospital, Boston.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.