Mutual regulation of conventional protein kinase C and a ubiquitin ligase complex
✍ Scribed by Munehiro Nakamura; Fuminori Tokunaga; Shin-ichi Sakata; Kazuhiro Iwai
- Book ID
- 116293775
- Publisher
- Elsevier Science
- Year
- 2006
- Tongue
- English
- Weight
- 799 KB
- Volume
- 351
- Category
- Article
- ISSN
- 0006-291X
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## Abstract **Background:** Recent studies have demonstrated that c‐Cbl functions as a ubiquitin‐protein ligase toward immune receptors and non‐receptor protein‐tyrosine kinase Syk by facilitating their ubiquitination and subsequent targeting to proteasomes. However, it was not clear whether Src fa
proto-oncogene that regulates the p53 tumor suppressor (Fang et al., 2000), and members of the IAP family Ubiquitin-protein ligases (E3s) regulate diverse celluof antiapoptotic proteins (Yang et al., 2000). lar processes by mediating protein ubiquitination. The The c-Cbl protein attenuates signaling