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Brd2/RING3 interacts with a chromatin-binding domain in the Kaposi's Sarcoma-associated herpesvirus latency-associated nuclear antigen 1 (LANA-1) that is required for multiple functions of LANA-1
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Viejo-Borbolla A Ottinger M Brüning E Bürger A König R Kati E Sheldon JA Schulz TF 《Journal of virology》2005,79(21):13618-13629
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P Vaudin R Delanoue I Davidson J Silber A Zider 《Development (Cambridge, England)》1999,126(21):4807-4816
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Bromodomain protein Brd4 binds to GTPase-activating SPA-1, modulating its activity and subcellular localization
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Farina A Hattori M Qin J Nakatani Y Minato N Ozato K 《Molecular and cellular biology》2004,24(20):9059-9069
Brd4 is a mammalian protein that contains a double bromodomain. It binds to chromatin and regulates cell cycle progression at multiple stages. By immunopurification and mass spectrometry, we identified a Rap GTPase-activating protein (GAP), signal-induced proliferation-associated protein 1 (SPA-1), as a factor that interacts with Brd4. SPA-1 localizes to the cytoplasm and to a lesser degree in the nucleus, while Brd4 resides in the nucleus. Bifluorescence complementation revealed that Brd4 and SPA-1 interact with each other in the nucleus of living cells. Supporting the functional importance of the interaction, Brd4 enhanced Rap GAP activity of SPA-1. Furthermore ectopic expression of SPA-1 and Brd4 redirected subcellular localization of the partner and disrupted normal cell cycle progression. These effects were, however, reversed by coexpression of the two proteins, indicating that a proper balance between Brd4 and SPA-1 in G2 is required for cell division. This work reveals a novel link between Brd4 and a GTPase-dependent mitogenic signaling pathway. 相似文献