Transrepression
In the field of molecular biology, transrepression is a process whereby one protein represses (i.e., inhibits) the activity of a second protein through a protein-protein interaction. Since this repression occurs between two different protein molecules (intermolecular), it is referred to as a trans-acting process. The protein that is repressed is usually a transcription factor whose function is to up-regulate (i.e., increase) the rate of gene transcription. Hence the net result of transrepression is down regulation of gene transcription. An example of transrepression is the ability of the glucocorticoid receptor to inhibit the transcriptional promoting activity of the AP-1 and NF-κB transcription factors. In addition to transactivation, transrepression is an important pathway for the anti-inflammatory effects of glucocorticoids. Other nuclear receptors such as LXR and PPAR have been demonstrated to also have the ability to transrepress the activity of other proteins.
In the field of molecular biology, transrepression is a process whereby one protein represses (i.e., inhibits) the activity of a second protein through a protein-protein interaction. Since this repression occurs between two different protein molecules (intermolecular), it is referred to as a trans-acting process.
The protein that is repressed is usually a transcription factor whose function is to up-regulate (i.e., increase) the rate of gene transcription. Hence the net result of transrepression is down regulation of gene transcription.
An example of transrepression is the ability of the glucocorticoid receptor to inhibit the transcriptional promoting activity of the AP-1 and NF-κB transcription factors.[1][2] In addition to transactivation, transrepression is an important pathway for the anti-inflammatory effects of glucocorticoids.[3][4] Other nuclear receptors such as LXR and PPAR have been demonstrated to also have the ability to transrepress the activity of other proteins.[5]
See also
[edit]References
[edit]- ^ Lucibello FC, Slater EP, Jooss KU, Beato M, Müller R (September 1990). "Mutual transrepression of Fos and the glucocorticoid receptor: involvement of a functional domain in Fos which is absent in FosB". EMBO J. 9 (9): 2827–34. doi:10.1002/j.1460-2075.1990.tb07471.x. PMC 551994. PMID 2118106.
- ^ Lin, Cw; Nakane, M; Stashko, M; Falls, D; Kuk, J; Miller, L; Huang, R; Tyree, C; Miner, Jn; Rosen, J; Kym, Pr; Coghlan, Mj; Carter, G; Lane, Bc (Aug 2002). "trans-Activation and repression properties of the novel nonsteroid glucocorticoid receptor ligand 2,5-dihydro-9-hydroxy-10-methoxy-2,2,4-trimethyl-5-(1-methylcyclohexen-3-y1)-1H-1benzopyrano3,4-fquinoline (A276575) and its four stereoisomers" (Free full text). Molecular Pharmacology. 62 (2): 297–303. doi:10.1124/mol.62.2.297. ISSN 0026-895X. PMID 12130681.
- ^ Pascual G, Glass CK (October 2006). "Nuclear receptors versus inflammation: mechanisms of transrepression". Trends Endocrinol. Metab. 17 (8): 321–7. doi:10.1016/j.tem.2006.08.005. PMID 16942889. S2CID 19612552.
- ^ Newton R, Holden NS (October 2007). "Separating transrepression and transactivation: a distressing divorce for the glucocorticoid receptor?". Mol. Pharmacol. 72 (4): 799–809. doi:10.1124/mol.107.038794. PMID 17622575. S2CID 52803631.
- ^ Ghisletti S, Huang W, Ogawa S, Pascual G, Lin ME, Willson TM, Rosenfeld MG, Glass CK (January 2007). "Parallel SUMOylation-dependent pathways mediate gene- and signal-specific transrepression by LXRs and PPARγ". Mol. Cell. 25 (1): 57–70. doi:10.1016/j.molcel.2006.11.022. PMC 1850387. PMID 17218271.
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