Phosphorylation regulates cullin-based ubiquitination in tumorigenesis
Cullin-RING ligases (CRLs) recognize and communicate with substrates for ubiquitination and degradation, and could be focused on disease treatment once the abnormal expression of substrates involves pathologic processes. Phosphorylation, either of substrates or receptors of CRLs, can transform their interaction. Phosphorylation-dependent ubiquitination and proteasome degradation influence various cellular processes and may lead to the appearance of various illnesses, most frequently tumorigenesis. These processes have the possibility for use for tumor intervention with the regulating those activities of related kinases, combined with the regulating the soundness of specific oncoproteins and tumor suppressors. This review describes the mechanisms and biological NSC 154020 functions of crosstalk between phosphorylation and ubiquitination, and more importantly its affect on tumorigenesis, to supply new directions and techniques for tumor therapy.