The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
The nuclear hormone receptor coactivator SRC-1 is a specific target of p300.
Open accessAbstract
p300 and its family member, CREB-binding protein (CBP), function as key transcriptional coactivators by virtue of their interaction with the activated forms of certain transcription factors. In a search for additional cellular targets of p300/CBP, a protein-protein cloning strategy, surprisingly identified SRC-1, a coactivator involved in nuclear hormone receptor transcriptional activity, as a p300/CBP interactive protein. p300 and SRC-1 interact, specifically, in vitro and they also form complexes in vivo. Moreover, we show that SRC-1 encodes a new member of the basic helix-loop-helix-PAS domain family and that it physically interacts with the retinoic acid receptor in response to hormone binding. Together, these results implicate p300 as a component of the retinoic acid signaling pathway, operating, in part, through specific interaction with a nuclear hormone receptor coactivator, SRC-1.
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Cites
The nuclear receptor superfamily: the second decade
Mangelsdorf, D. J., Thummel, C., Beato, M., Herrlich, P., Schütz, G., Umesono, K., Blumberg, B., Kastner, P., Mark, M., Chambon, P., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90199-x · Cited by 6,964
Phosphorylated CREB binds specifically to the nuclear protein CBP
Chrivia, J. C., Kwok, R. P. S., Lamb, N., Hagiwara, M., Montminy, M. R., & Goodman, R. H. (1993) · Nature · doi:10.1038/365855a0 · Cited by 2,052
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E1A-associated p300 and CREB-associated CBP belong to a conserved family of coactivators
Arany, Z. (1994) · Cell · doi:10.1016/0092-8674(94)90127-9 · Cited by 444
Cited by
The coregulator exchange in transcriptional functions of nuclear receptors
Glass, C. K., & Rosenfeld, M. G. (2000) · Genes & Development · doi:10.1101/gad.14.2.121 · Cited by 2,233
A signature motif in transcriptional co-activators mediates binding to nuclear receptors
Heery, D. M., Kalkhoven, E., Hoare, S., & Parker, M. G. (1997) · Nature · doi:10.1038/42750 · Cited by 2,128
Physiological and Molecular Basis of Thyroid Hormone Action
Yen, P. M. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.3.1097 · Cited by 2,011
AIB1, a Steroid Receptor Coactivator Amplified in Breast and Ovarian Cancer
Anzick, S. L., Kononen, J., Walker, R. L., Azorsa, D. O., Tanner, M. M., Guan, X.-Y., Sauter, G., Kallioniemi, O.-P., Trent, J. M., & Meltzer, P. S. (1997) · Science · doi:10.1126/science.277.5328.965 · Cited by 1,639
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
Metadata
- Authors
- Yao, T. P., Ku, G., Zhou, N., Scully, R., & Livingston, D. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1996-10
- Volume
- 93
- Issue
- 20
- Pages
- 10626-10631
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1974127600
- Cited by
- 453
- References
- 4
- FWCI
- 18.80
- Type
- journal article
- Language
- en
- Open access
- green
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- Yao, T. P., Ku, G., Zhou, N., Scully, R., & Livingston, D. M. (1996). The nuclear hormone receptor coactivator SRC-1 is a specific target of p300. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.93.20.10626
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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