Soubeyran Philippe, Barac Ana, Szymkiewicz Iwona, Dikic Ivan
Ludwig Institute for Cancer Research, Box 595, Husargatan 3, Uppsala, S-75124, Sweden.
Biochem J. 2003 Feb 15;370(Pt 1):29-34. doi: 10.1042/BJ20021539.
The mechanisms leading to the ubiquitination and degradation of the activated c-Abl kinase have not yet been identified. We found that the multi-adaptor protein ArgBP2 links c-Abl to the ubiquitin ligase Cbl. Phosphorylation of Cbl and ArgBP2 by c-Abl resulted in the stabilization of their interactions, thus facilitating Cbl-induced ubiquitination and subsequent degradation of c-Abl and ArgBP2.
导致活化的c-Abl激酶泛素化和降解的机制尚未明确。我们发现多接头蛋白ArgBP2将c-Abl与泛素连接酶Cbl相连。c-Abl对Cbl和ArgBP2的磷酸化导致它们相互作用的稳定,从而促进Cbl诱导的c-Abl和ArgBP2的泛素化及随后的降解。