Tripartite motif-containing 24 (TRIM24) also known as transcriptional intermediary factor 1α (TIF1α) is a protein that, in humans, is encoded by the TRIM24gene.[5][6][7]
Function
The protein encoded by this gene mediates transcriptional control by interaction with the activation function 2 (AF2) region of several nuclear receptors, including the estrogen, retinoic acid, and vitamin D3 receptors. The protein localizes to nuclear bodies and is thought to associate with chromatin and heterochromatin-associated factors. The protein is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains – a RING, a B-box type 1 and a B-box type 2 – and a coiled-coil region. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.[5]
^Le Douarin B, Nielsen AL, You J, Chambon P, Losson R (May 1997). "TIF1 alpha: a chromatin-specific mediator for the ligand-dependent activation function AF-2 of nuclear receptors?". Biochem. Soc. Trans. 25 (2): 605–12. doi:10.1042/bst0250605. PMID9191165.
^Peng, Hongzhuang; Feldman Irina; Rauscher Frank J (July 2002). "Hetero-oligomerization among the TIF family of RBCC/TRIM domain-containing nuclear cofactors: a potential mechanism for regulating the switch between coactivation and corepression". J. Mol. Biol. 320 (3). England: 629–44. doi:10.1016/S0022-2836(02)00477-1. ISSN0022-2836. PMID12096914.
^Lee, Wen-yi; Noy Noa (February 2002). "Interactions of RXR with coactivators are differentially mediated by helix 11 of the receptor's ligand binding domain". Biochemistry. 41 (8). United States: 2500–8. doi:10.1021/bi011764+. ISSN0006-2960. PMID11851396.
Further reading
Le Douarin B, Nielsen AL, You J, et al. (1997). "TIF1 alpha: a chromatin-specific mediator for the ligand-dependent activation function AF-2 of nuclear receptors?". Biochem. Soc. Trans. 25 (2): 605–12. doi:10.1042/bst0250605. PMID9191165.
Remboutsika E, Lutz Y, Gansmuller A, et al. (1999). "The putative nuclear receptor mediator TIF1alpha is tightly associated with euchromatin". J. Cell Sci. 112 (11): 1671–83. doi:10.1242/jcs.112.11.1671. PMID10318760.
Klugbauer S, Rabes HM (1999). "The transcription coactivator HTIF1 and a related protein are fused to the RET receptor tyrosine kinase in childhood papillary thyroid carcinomas". Oncogene. 18 (30): 4388–93. doi:10.1038/sj.onc.1202824. PMID10439047. S2CID2166439.
Zhong S, Delva L, Rachez C, et al. (1999). "A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins". Nat. Genet. 23 (3): 287–95. doi:10.1038/15463. PMID10610177. S2CID23613492.
Lee WY, Noy N (2002). "Interactions of RXR with coactivators are differentially mediated by helix 11 of the receptor's ligand binding domain". Biochemistry. 41 (8): 2500–8. doi:10.1021/bi011764+. PMID11851396.
Peng H, Feldman I, Rauscher FJ (2002). "Hetero-oligomerization among the TIF family of RBCC/TRIM domain-containing nuclear cofactors: a potential mechanism for regulating the switch between coactivation and corepression". J. Mol. Biol. 320 (3): 629–44. doi:10.1016/S0022-2836(02)00477-1. PMID12096914.
