Cullin-7 (CUL7)

Cullin-7 (CUL7) is a scaffold protein that assembles E3 ubiquitin ligase complexes, serving a central role in the ubiquitin-proteasome system by targeting proteins for degradation via ubiquitination[1][2][4]. It interacts with various adaptor proteins (e.g., Skp1, F-box proteins such as Fbxw8 and Fbxw11, and ROC1/Rbx1) to confer substrate specificity and can bind and mono- or di-ubiquitinate the tumor suppressor p53, antagonizing its function and thereby promoting cell proliferation and survival[2][3][4]. CUL7 is essential for normal organismal growth and cell cycle progression; deleterious mutations cause 3-M syndrome, a primordial growth disorder marked by severe pre- and postnatal growth failure and skeletal anomalies, often due to impaired assembly and function of the E3 ligase complex[1][2]. In cancer biology, CUL7 acts in a context-dependent manner, either promoting or inhibiting tumorigenesis; its overexpression is linked to aggressive cancers such as breast cancer, where it promotes proliferation, invasion, and disrupts microtubule dynamics[4][5]. Despite its recognized roles, CUL7 is not currently an established drug target, and no approved drugs specifically target this protein[4][6].

Other names

CUL7KIAA0076CUL-7dJ20C7.53M1cullin 7

Not currently targeted by approved drugs; theoretical mechanisms would include inhibition of E3 ligase activity or blockade of scaffold interactions for purposes such as anti-cancer therapy[4].