Cullin (CUL) proteins have critical roles in development and cancer, however few studies on CUL7 have been reported due to its characteristic molecular structure. CUL7 forms a complex with the ROC1 ring finger protein, and only two F-box proteins Fbxw8 and Fbxw11 have been shown to bind to CUL7. Interestingly, CUL7 can interact with its substrates by forming a novel complex that is independent of these two F-box proteins. The biological implications of CUL-ring ligase 7 (CRL7) suggest that the CRL7 may not only perform a proteolytic function but may also play a non-proteolytic role. Among the existing studied CRL7-based E3 ligases, CUL7 exerts both tumor promotion and suppression in a context-dependent manner. Currently, the mechanism of CUL7 in cancer remains unclear, and no studies have addressed potential therapies targeting CUL7. Consistent with the roles of the various CRL7 adaptors exhibit, targeting CRL7 might be an effective strategy for cancer prevention and treatment. We systematically describe the recent major advances in understanding the role of the CUL7 E3 ligase in cancer and further summarize its potential use in clinical therapy.

Cullin（CUL）蛋白在发育和癌症中起着至关重要的作用，但是由于CUL7的特征分子结构，因此尚无关于CUL7的研究报道。CUL7与ROC1无名指蛋白形成复合物，并且仅两个F-box蛋白Fbxw8和Fbxw11与CUL7结合。有趣的是，CUL7可以通过形成独立于这两个F-box蛋白的新型复合物来与其底物相互作用。CUL环连接酶7（CRL7）的生物学意义表明，CRL7不仅可以发挥蛋白水解功能，而且还可以发挥非蛋白水解作用。在现有研究的基于CRL7的E3连接酶中，CUL7以依赖于上下文的方式发挥肿瘤的促进和抑制作用。目前，CUL7在癌症中的机制尚不清楚，并且没有研究针对靶向CUL7的潜在疗法。与各种CRL7衔接子的作用一致，靶向CRL7可能是癌症预防和治疗的有效策略。我们系统地描述了最近的主要进展，以了解CUL7 E3连接酶在癌症中的作用，并进一步总结了其在临床治疗中的潜在用途。