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Background
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CHIP is an E3 ligase for nNOS whose action is facilitated by (and possibly requires) its interaction with nNOS-bound hsp70. Co-chaperone CHIP, possibly with another E3 ligase(s), modulates the ubiquitylation of mutant Cu/Zn-superoxide dismutase and renders them more susceptible for proteasomal degradation. CHIP functions as a negative regulator of AR transcriptional activity by promoting AR degradation. CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. CHIP can interact with the Smad1/Smad4 proteins and block BMP signal transduction through the ubiquitin-mediated degradation of Smad proteins. CHIP E3 controls both the association of Hsp70/Hsp90 chaperones with ErbB2 and the down-regulation of ErbB2 induced by inhibitors of Hsp90. CHIP is associated with Parkin and enhances its ubiquitin ligase activity related to Parkinson's disease.
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Background
References
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- Peng,H.M., et al. J. Biol. Chem. 279 (51), 52970-52977 (2004)
- Alberti,S., et al. Mol. Biol. Cell 15 (9), 4003-4010 (2004)
- Beausoleil,S.A., et al. PNAS 101 (33), 12130-12135 (2004)
- He,B., et al. J. Biol. Chem. 279 (29), 30643-30653 (2004)
- Petrucelli,L., et al. Hum. Mol. Genet. 13 (7), 703-714 (2004)
- Shimura,H., et al. J. Biol. Chem. 279 (6), 4869-4876 (2004)
- Li,L., et al. Mol. Cell. Biol. 24 (2), 856-864 (2004)
- Zhou,P., et al. J. Biol. Chem. 278 (16), 13829-13837 (2003)
- Imai,Y., et al. Mol. Cell 10 (1), 55-67 (2002)
- Ballinger,C.A., et al. Mol. Cell. Biol. 19 (6), 4535-4545 (1999)
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