Becn1, encoding the Beclin-1 protein, is a well-established regulator of the autophagic pathway and a mammalian orthologue of the yeast ATG6 gene [7]. As a core component of the class III phosphatidylinositol 3-kinase complexes, it mediates autophagy, which is crucial for maintaining cellular homeostasis. Besides autophagy, Becn1 is also involved in processes like apoptosis, embryogenesis, and innate immune responses, and is implicated in diseases such as cancer, neurological disorders, and viral infections [7,8].

CUL3, an E3 ubiquitin ligase, can interact with BECN1, promoting its K48-linked ubiquitination and degradation, thus inhibiting autophagy and promoting tumor progression in breast and ovarian cancer [1]. IL-6 activates autophagy through the IL-6/JAK2/BECN1 pathway in colorectal cancer, with JAK2 phosphorylating BECN1 at Y333, which is crucial for BECN1 activation and IL-6-induced autophagy [2]. AMPK-mediated phosphorylation of BECN1 at Ser90/93/96 promotes ferroptosis by directly blocking system Xc-activity [3]. VCP/p97 UFMylation stabilizes BECN1 and facilitates autophagy initiation [4]. TRIM59 regulates autophagy by modulating both the transcription and the ubiquitination of BECN1 in non-small cell lung cancer [5]. USP19 affects the ubiquitination of BECN1, promoting autophagosome formation and inhibiting DDX58/RIG-I-mediated type I interferon signaling [6].

In conclusion, Becn1 is a key regulator of autophagy and is involved in multiple biological processes and disease conditions. Studies on Becn1, including those using gene-knockout or conditional-knockout mouse models, have enhanced our understanding of its role in diseases such as cancer, neurodegenerative disorders, and viral infections, providing potential therapeutic strategies.