Nuclear Receptor Signaling

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There are three members of the steroid receptor co-activator (SRC) family of proteins: SRC-1 (NCoA-1), SRC-2 (TIF2/GRIP1/NCoA-2) and SRC-3 (ACTR/pCIP/RAC3/TRAM-1/AIB1). The SRC family members all share significant structural homology and function in a similar fashion to stimulate transcription mediated by nuclear hormone receptors and other transcriptional activators such as STAT3, NF-κB, E2F1 and p53 (1-4). Two SRC proteins, SRC-1 and SRC-3, function as histone acetyltransferases (5,6). In addition, all three family members can recruit other histone acetyltransferases (CBP/p300, PCAF) and histone methyltransferases (PRMT1, CARM1) to target promoters and cooperate to enhance expression of many genes (5-8). The SRC proteins play important roles in multiple physiological processes including cell proliferation, cell survival, somatic cell growth, mammary gland development, female reproductive function and vasoprotection (9). SRC-1 and SRC-3 are conduits for kinase-mediated growth factor signaling to the estrogen receptor and other transcriptional activators. Seven SRC-1 phosphorylation sites and six SRC-3 phosphorylation sites have been identified, which are induced by steroids, cytokines and growth factors and involve multiple kinase signaling pathways (9-11). All three SRC family members are associated with increased activity of nuclear receptors in breast, prostate and ovarian carcinomas. In addition, SRC-3 is frequently amplified or over-expressed in a number of cancers (12), and SRC-1/PAX3 and SRC-2/MYST3 translocations are found associated with rhabdomyosarcoma and acute myeloid leukemia, respectively (13,14).

Phosphorylation of Thr24 of SRC-3 proteins can be induced by stimulation with EGF. Phosphorylated SRC-3 translocates from the cytoplasm to the nucleus where it interacts with other transcription factors and steroid hormone receptors and regulates gene expression (15).

1. Giraud, S. et al. (2002) J. Biol. Chem. 277, 8004-8011.
2. Na, S.Y. et al. (1998) J. Biol. Chem. 273, 10831-10834.
3. Louie, M.C. et al. (2004) Mol. Cell Biol. 24, 5157-5171.
4. Lee, S.K. et al. (1999) Mol. Endocrinol. 13, 1924-1933.
5. Spencer, T.E. et al. (1997) Nature 389, 194-198.
6. Chen, H. et al. (1997) Cell 90, 569-580.
7. Koh, S.S. et al. (2001) J. Biol. Chem. 276, 1089-1098.
8. Chen, D. et al. (1999) Science 284, 2174-2177.
9. Wu, R.C. et al. (2004) Mol. Cell 15, 937-949.
10. Rowan, B.G. et al. (2000) J. Biol. Chem. 275, 4475-4483.
11. Zhou, H.J. et al. (2005) Cancer Res. 65, 7976-7983.
12. Torres-Arzayus, M.I. et al. (2004) Cancer Cell 6, 263-274.
13. Wachtel, M. et al. (2004) Cancer Res. 64, 5539-5545.
14. Deguchi, K. et al. (2003) Cancer Cell 3, 259-271.
15. Amazit, L. et al. (2007) Mol. Cell Biol. 27, 6913-6932.

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Phospho-SRC-3 (Thr24) Antibody

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