The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Cabin1 Represses MEF2-Dependent Nur77 Expression and T Cell Apoptosis by Controlling Association of Histone Deacetylases and Acetylases with MEF2
Open accessAbstract
TCR signaling leading to thymocyte apoptosis is mediated through the expression of the Nur77 family of orphan nuclear receptors. MEF2 has been shown to be the major transcription factor responsible for calcium-dependent Nur77 transcription. Cabin1 was recently identified as a transcriptional repressor of MEF2, which can be released from MEF2 in a calcium-dependent fashion. The molecular basis of repression of MEF2 by Cabin1, however, has remained unknown. We report that Cabin1 represses MEF2 by two distinct mechanisms. Cabin1 recruits mSin3 and its associated histone deacetylases 1 and 2; Cabin1 also competes with p300 for binding to MEF2. Thus, activation of MEF2 and the consequent transcription of Nur77 are controlled by the association of MEF2 with the histone deacetylases via the calcium-dependent repressor Cabin1.
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Cites
Histone acetylation in chromatin structure and transcription
Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829
Nuclear Receptor Repression Mediated by a Complex Containing SMRT, mSin3A, and Histone Deacetylase
Nagy, L., Kao, H.-Y., Chakravarti, D., Lin, R. J., Hassig, C. A., Ayer, D. E., Schreiber, S. L., & Evans, R. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80218-4 · Cited by 1,230
Three proteins define a class of human histone deacetylases related to yeast Hda1p
Grozinger, C. M., Hassig, C. A., & Schreiber, S. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4868 · Cited by 770
Histone Deacetylases and SAP18, a Novel Polypeptide, Are Components of a Human Sin3 Complex
Zhang, Y., Iratni, R., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (1997) · Cell · doi:10.1016/s0092-8674(00)80216-0 · Cited by 578
MEF‐2 function is modified by a novel co‐repressor, MITR
Sparrow, D. B., Miska, E. A., Langley, E., Reynaud‐Deonauth, S., Kotecha, S., Towers, N., Spohr, G., Kouzarides, T., & Mohun, T. J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.18.5085 · Cited by 196
Cited by
Frequent mutation of histone-modifying genes in non-Hodgkin lymphoma
Morin, R. D., Mendez-Lago, M., Mungall, A. J., Goya, R., Mungall, K. L., Corbett, R. D., Johnson, N. A., Severson, T. M., Chiu, R., Field, M., et al. (2011) · Nature · doi:10.1038/nature10351 · Cited by 1,614
MEF2: a central regulator of diverse developmental programs
Potthoff, M. J., & Olson, E. N. (2007) · Development · doi:10.1242/dev.008367 · Cited by 834
MEF2: a calcium-dependent regulator of cell division, differentiation and death
McKinsey, T. A., Zhang, C. L., & Olson, E. N. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)02031-x · Cited by 687
Greer, P. L., & Greenberg, M. E. (2008) · Neuron · doi:10.1016/j.neuron.2008.09.002 · Cited by 661
Class II histone deacetylases: versatile regulators
Verdin, E., Dequiedt, F., & Kasler, H. G. (2003) · Trends in Genetics · doi:10.1016/s0168-9525(03)00073-8 · Cited by 664
Metadata
- Authors
- Youn, H.-D., & Liu, J. O.
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2000-07
- Volume
- 13
- Issue
- 1
- Pages
- 85-94
- ISSN
- 1074-7613 (ISSN-L)
- OpenAlex
- W1992263554
- Cited by
- 161
- References
- 6
- FWCI
- 4.17
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Cabin1 Represses MEF2-Dependent Nur77 Expression and T Cell Apoptosis by Controlling Association of Histone Deacetylases and Acetylases with MEF2. https://app.cochat.ai/papers/10.1016/s1074-7613(00)00010-8
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- Youn, H.-D., & Liu, J. O. (2000). Cabin1 Represses MEF2-Dependent Nur77 Expression and T Cell Apoptosis by Controlling Association of Histone Deacetylases and Acetylases with MEF2. Immunity. https://doi.org/10.1016/s1074-7613(00)00010-8
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