von Dott. Raffaele La Montagna
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| [1.] Rlm/Fragment 015 01 - Diskussion Zuletzt bearbeitet: 2014-12-10 23:37:12 Hindemith | Fragment, Gesichtet, Rlm, SABiosciences Androgen Signaling 2009, SMWFragment, Schutzlevel sysop, Verschleierung |
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| Untersuchte Arbeit: Seite: 15, Zeilen: 1 ff. (entire page) |
Quelle: SABiosciences Androgen Signaling 2009 Seite(n): online, Zeilen: - |
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| The ATPase/ Kinase TFIIE and helicase TFIIH are than recruited to RNA Pol II to facilitate DNA strand separation before transcription initiation. TFIIE and TFIIF are acetylated by p300 and p/CAF. Ubiquitin ligase activity has been identified for two AR coactivators, ARA54 and E6-AP.The coactivators with ubiquitin ligase activity contribute to nuclear receptor transactivation through targeting the degradation of corepressor. AR can also interact with a number of transcription factor including Activator Protein-1,SMAD3( Sma and Mad Related Family),NF-KappaB (Nuclear Factor-KappaB), SRY (Sex-determining Region-Y), and the Ets family of transcription factors.
Transcriptional corepression of androgen-bound AR can be attributed to three corepressors: cyclin D1, calreticulin and HBO1.Cyclin-D1 inhibits AR transactivation through a mechanism independent of its function in cell cycle regulation (7). The calcium –binding protein calreticulinis [sic] localized to the endoplasmic reticulum and in the nucleus and has also been characterized as corepressor of AR. 7) Bakin RE, Gioeli D, Sikes RA, Bissonette EA, Weber MJ 2003 Constitutive activation of the ras/mitogen-activated protein kinase signaling pathway promotes androgen hypersensitivity in LNCaP prostate cancer cells. Cancer Res 63:1981–1989 |
The ATPase and kinase TFIIE and the helicase TFIIH are then recruited to RNA Pol II to facilitate DNA strand separation before transcription initiation. TFIIE and TFIIF recruitment to RNA pol II are acetylated by p300 and p/CAF (Ref.2). Ubiquitin ligase activity has been identified for two AR coactivators, ARA54 and E6-AP. The coactivators with ubiquitin ligase activity contribute to nuclear receptor transcription through targeting the degradation of corepressors. AR can also interact with a number of transcription factors including Activator Protein-1, SMAD3 (Sma and Mad Related Family), NF-KappaB (Nuclear Factor-KappaB), SRY (Sex-determining Region-Y), and the Ets family of transcription factors.
Transcriptional corepression of androgen-bound AR can be attributed to three corepressors: cyclin-D1, calreticulin and HBO1. Cyclin-D1 inhibits AR transactivation through a mechanism independent of its function in cell cycle regulation (Ref.4). The calcium-binding protein calreticulin is localized to the endoplasmic reticulum and nucleus and has also been characterized as a corepressor of AR. 2. Lee DK, Chang C Molecular communication between androgen receptor and general transcription machinery. J Steroid Biochem Mol Biol. 2003 Jan;84(1):41-9. 4. Petre CE, Wetherill YB, Danielsen M, Knudsen KE Cyclin D1: mechanism and consequence of androgen receptor co-repressor activity. J Biol Chem. 2002 Jan 18;277(3):2207-15. Epub 2001 Nov 19. |
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Letzte Bearbeitung dieser Seite: durch Benutzer:Hindemith, Zeitstempel: 20141210233856