2004 Fiscal Year Final Research Report Summary
Cloning and characterization of a novel coactivator, ANT-1, for androgen receptor AF-1 domain
| Project/Area Number |
14571068
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Endocrinology
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| Research Institution | Kyushu University |
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Principal Investigator |
GOTO Kiminobu KYUSHU UNIVERSITY, University Hospital, Research Associate, 大学病院, 助手 (90284512)
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| Co-Investigator(Kenkyū-buntansha) |
YANASE Toshihiko KYUSHU UNIVERSITY, Graduate School of Medical Sciences, Associate Professor, 医学研究院, 助教授 (30239818)
NAWATA Hajime KYUSHU UNIVERSITY, Graduate School of Medical Sciences, Professor, 医学研究院, 教授 (10038820)
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| Project Period (FY) |
2002 – 2004
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| Keywords | androgen receptor / transcriptional coactivator / activation function-1 / confocal microscopy / nuclear localization signal / subnuclear compartment / mammalian two-hybrid |
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| Research Abstract |
We have previously identified a novel coactivator for the activation function-1 (AF-1) domain of the androgen receptor (AR). This coactivator, named androgen receptor N-terminal domain transactivating protein-1 (ANT-1), is unique, since the ANT-1 is a component of U5 small nuclear ribonucleoparticle (snRNP), thus raising the possibility that the AR-AF-1 may be involved in the transcription-splicing coupling via ANT-1. We identified four distinguished functional domains required for ANT-1 to play a role as a unique coactivator for AR ; which were transactivating domain, AR-AF-1 binding domain, nuclear translocation signal domain, and intranuclear speckle formation domain. In the ANT-1, consisted of 941 amino acid (aa) residues, about two thirds of the molecule from 291 aa to the C-terminal end contains 19 tetratricopeptide repeat (TPR) motifs which has been speculated to play a role in protein-protein interactions. Interestingly both AR-AF-1 binding domain and the speckle formation domain of ANT-1 were assigned within this long region containing multiple TPR motifs, while transactivating domain and the nuclear translocation signal resided only in the 1 to 172 aa residues. Furthermore, the transactivating domain of ANT-1 was not specific for the AR, that is it enhanced even non-specific viral prompters. The receptor specificity of ANT-1 transactivation was simply determined by the TPR containing region. These results indicated that the ANT-1 actually contained four distinguished intramolecular functional domains, thus suggesting that the ANT-1 play a significant role in vivo.
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Research Products
(8 results)
