Linked Life Data

15031286

Source:http://linkedlifedata.com/resource/pubmed/id/15031286

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2004-5-17
pubmed:abstractText
Upon binding to androgen, androgen receptor (AR) can activate expression of target genes through its direct binding to the androgen-responsive elements (AREs), which are located within the target gene promoters and/or enhancers. A number of cellular proteins have been identified as co-regulators to regulate this transactivation process. One common structural feature among these co-regulators is the presence of the LXXLL motif (X, any amino acid), the so-called nuclear receptor (NR) box, through which binding of these regulatory proteins to AR occurs. We have recently shown that Tip110 functions to potentiate the transactivation activity of human immunodeficiency virus type I (HIV-1) Tat protein. In this study, we report that Tip110 is a potent AR-binding protein that can suppress AR activity. Tip110 bound to AR in an NR box-dependent manner and inhibited AREs-mediated reporter gene expression. The inhibitory effects were abolished by removal of the NR box. Moreover, knock-down of the constitutive Tip110 expression significantly augmented AR transcriptional activation. In agreement with these findings, Tip110 overexpression blocked the prostate-specific antigen (PSA) gene, a well characterized target gene of AR from expression in LNCaP cells. Further analysis revealed that Tip110 prevented the complex formation between AR and AREs. Taken together, these results indicate that Tip110 is a negative regulator of AR transcriptional activation, and may be directly involved in AR-related developmental, physiological, and pathological processes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21766-73
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15031286-Amino Acid Motifs, pubmed-meshheading:15031286-Antigens, Neoplasm, pubmed-meshheading:15031286-Binding Sites, pubmed-meshheading:15031286-Blotting, Northern, pubmed-meshheading:15031286-Blotting, Western, pubmed-meshheading:15031286-Cell Line, pubmed-meshheading:15031286-Cell Line, Tumor, pubmed-meshheading:15031286-Cell Nucleus, pubmed-meshheading:15031286-Glutathione Transferase, pubmed-meshheading:15031286-Humans, pubmed-meshheading:15031286-Mutation, pubmed-meshheading:15031286-Plasmids, pubmed-meshheading:15031286-Precipitin Tests, pubmed-meshheading:15031286-Prostate-Specific Antigen, pubmed-meshheading:15031286-Protein Binding, pubmed-meshheading:15031286-Protein Structure, Tertiary, pubmed-meshheading:15031286-RNA, pubmed-meshheading:15031286-RNA, Messenger, pubmed-meshheading:15031286-RNA-Binding Proteins, pubmed-meshheading:15031286-Receptors, Androgen, pubmed-meshheading:15031286-Recombinant Proteins, pubmed-meshheading:15031286-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:15031286-Transcriptional Activation
pubmed:year
2004
pubmed:articleTitle
Tip110, the human immunodeficiency virus type 1 (HIV-1) Tat-interacting protein of 110 kDa as a negative regulator of androgen receptor (AR) transcriptional activation.
pubmed:affiliation
Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.