| Modification Notes |
Transcriptional intermediary factor 1-å (TIF1å) mediates transcriptional events by interactions with the AF2 region of several nuclear receptors, such as the estrogen, retinoic acid, and vitamin D3 receptors. TIF1å localizes to nuclear bodies and is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains (RING, B-box type 1 and B-box type 2) and a coiled-coil region. TIF1∫ is also a member of the TRIM family that contains both a Cys/His PHD finger and bromodomain that form a cooperative unit required for transcriptional repression. TIF1∫ mediates transcriptional control by interaction with the Kruppel-associated box (KRAB) repression domain found in many transcription factors and by binding DNA via its zinc finger. TIF1© has a similar structure to the previous two TRIM members, though it presents several functional differences. TIF1© interacts with the Smad2/3 transcription factor in hematopoietic, mesenchymal, and epithelial cell types to mediate different transcriptional effects in response to TGF∫. |