Activation function-1 domain of androgen receptor contributes to the interaction between two distinct subnuclear compartments

Kiminobu Goto, Yue Zhao, Masayuki Saito, Arihiro Tomura, Hidetaka Morinaga, Masatoshi Nomura, Taijiro Okabe, Toshihiko Yanase, Ryoichi Takayanagi, Hajime Nawata

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The nucleus contains different sets of functional compartments often called "speckles". The splicing factor compartment (SFC) has been speculated to consist of SFs and transcription factors, which thus make transcription-splicing coupling possible at the periphery of SFC. Androgen receptor (AR), as well as glucocorticoid receptor (GR), is unique since most, if not all, of its activities are mediated via the constitutive activity of the activation function-1 (AF-1) function. Transcriptionally active AR produces 250-400 subnuclear fine speckles11 shared with GR or estrogen receptor (ER), which colocalize with chiefly activation function-2 (AF-2)-interacting p160 family- or CBP-related speckles. We herein report the isolation of ANT-1 (AR N-terminal domain (NTD) transactivating protein-1) enhancing autonomous AF-1 transactivation function of AR or GR, but not of estrogen receptor α (ERα). The ANT-1 was identical to a binding protein of human splicing factor U5 snRNP (U5 snRNP-associated protein). ANT-1 was compartmentalized into 15-20 coarse SFC speckles which were spatially distinct from but surrounded by the AR compartments. Our results suggest that ANT-1 may play a key role in the molecular interaction between two spatially distinct subnuclear compartments in a receptor-specific fashion, and thereby induce the strong autonomous transactivation functions either of AR- or GR-AF-1.

Original languageEnglish
Pages (from-to)201-208
Number of pages8
JournalJournal of Steroid Biochemistry and Molecular Biology
Volume85
Issue number2-5
DOIs
Publication statusPublished - Jan 1 2003

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Androgen Receptors
Chemical activation
Glucocorticoid Receptors
U5 Small Nuclear Ribonucleoproteins
Speckle
Estrogen Receptors
Transcriptional Activation
Protein Splicing
Molecular interactions
Transcription
Carrier Proteins
Transcription Factors
Proteins
RNA Splicing Factors

All Science Journal Classification (ASJC) codes

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Endocrinology
  • Clinical Biochemistry
  • Cell Biology

Cite this

Activation function-1 domain of androgen receptor contributes to the interaction between two distinct subnuclear compartments. / Goto, Kiminobu; Zhao, Yue; Saito, Masayuki; Tomura, Arihiro; Morinaga, Hidetaka; Nomura, Masatoshi; Okabe, Taijiro; Yanase, Toshihiko; Takayanagi, Ryoichi; Nawata, Hajime.

In: Journal of Steroid Biochemistry and Molecular Biology, Vol. 85, No. 2-5, 01.01.2003, p. 201-208.

Research output: Contribution to journalArticle

Goto, K, Zhao, Y, Saito, M, Tomura, A, Morinaga, H, Nomura, M, Okabe, T, Yanase, T, Takayanagi, R & Nawata, H 2003, 'Activation function-1 domain of androgen receptor contributes to the interaction between two distinct subnuclear compartments', Journal of Steroid Biochemistry and Molecular Biology, vol. 85, no. 2-5, pp. 201-208. https://doi.org/10.1016/S0960-0760(03)00196-1
Goto, Kiminobu ; Zhao, Yue ; Saito, Masayuki ; Tomura, Arihiro ; Morinaga, Hidetaka ; Nomura, Masatoshi ; Okabe, Taijiro ; Yanase, Toshihiko ; Takayanagi, Ryoichi ; Nawata, Hajime. / Activation function-1 domain of androgen receptor contributes to the interaction between two distinct subnuclear compartments. In: Journal of Steroid Biochemistry and Molecular Biology. 2003 ; Vol. 85, No. 2-5. pp. 201-208.
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