CBL neddylates TGFBR2

CBL neddylates TGFBR2 on lysine residues K556 and K567. The E3 ubiquitin ligase activity of CBL is necessary for this modification, and the kinase activity of TGFBR2 is also required. CBL-mediated neddylation prolongs the half-life of TGFBR2, thereby enhancing signaling by the TGF-beta receptor complex. CBLB, a CBL-related protein, may cooperate with CBL in TGFBR2 neddylation (Zuo et al. 2013).

CBL蛋白通过在赖氨酸残基K556和K567上 neddylation TGFBR2，此过程依赖于CBL的E3泛素连接酶活性，并需TGFBR2的激酶活性。CBL介导的 neddylation 可延长TGFBR2的半衰期，从而增强TGF-β受体复合体的信号传导。CBLB，一种与CBL相关的蛋白，可能与CBL协同作用以促进TGFBR2的neddylation（Zuo等，2013年）。