[HTML][HTML] The tyrosine kinase c-Abl protects c-Jun from ubiquitination-mediated degradation in T cells
B Gao, SM Lee, D Fang - Journal of Biological Chemistry, 2006 - ASBMB
The cross-talk of ubiquitination with other types of posttranscriptional modifications, such as
phosphorylation, regulates the stability of many proteins. We have previously demonstrated
that c-Jun is a substrate of Itch, a HECT-type E3 ubiquitin ligase. c-Jun is also a substrate of
the tyrosine kinase c-Abl. Here we report that genetic ablation of c-Abl accelerated c-Jun
degradation. Phosphorylation of the tyrosine within the PPXY motif by c-Abl inhibited c-Jun
ubiquitination and its binding by Itch. The nuclear localization of c-Abl, triggered by T-cell …
phosphorylation, regulates the stability of many proteins. We have previously demonstrated
that c-Jun is a substrate of Itch, a HECT-type E3 ubiquitin ligase. c-Jun is also a substrate of
the tyrosine kinase c-Abl. Here we report that genetic ablation of c-Abl accelerated c-Jun
degradation. Phosphorylation of the tyrosine within the PPXY motif by c-Abl inhibited c-Jun
ubiquitination and its binding by Itch. The nuclear localization of c-Abl, triggered by T-cell …