Elob, also known as Elongin B, is a pivotal element in the ELOB/c-Cullin2/5-SOCS-box E3 ubiquitin-protein ligase complex. It is involved in catalyzing the ubiquitination and subsequent degradation of a broad spectrum of target proteins, and participates in multiple biological pathways such as cell cycle, DNA replication, proteasome, and PI3K-Akt signaling pathway [3]. Elongin B forms a heterodimer with Elongin C (ELOC), and this dimer binds to a BC-box motif, being essential for cancer cell growth [1].

In breast cancer, down-regulation of Elob significantly suppresses the proliferation of breast cancer cells both in vivo and in vitro. Elob, as the core element of Cullin2-RBX1-ELOB E3 ligase (CRL2) complex, regulates the ubiquitination and degradation of oncoprotein p14/ARF [3]. In triple-negative breast cancer, high Elob expression is associated with poor prognosis in patients receiving radiation therapy. Targeting Elob can modulate mitochondrial function and enhance radiosensitivity [4]. In colorectal cancer, Elob is part of a larger functional complex (USP51/VHL/CUL2/ELOB/ELOC/RBX1) that regulates the ubiquitin-dependent proteasomal degradation of HIF1A, and USP51 promotes colorectal cancer stemness and chemoresistance [2].

In conclusion, Elob plays a crucial role in cancer-related biological processes such as cell proliferation, apoptosis, and response to radiotherapy. Its involvement in the ubiquitination and degradation of key proteins in cancer cells makes it a potential therapeutic target for breast cancer, triple-negative breast cancer, and colorectal cancer. The study of Elob knockout or conditional knockout models in these contexts could further reveal its underlying molecular mechanisms and offer new strategies for cancer treatment.