The Beclin 1 network plays a central role in regulating autophagy, a process essential for cellular homeostasis. Beclin 1, the mammalian orthologue of yeast Atg6, interacts with various cofactors to form core complexes that promote autophagosome formation and maturation. These complexes include the Beclin 1-Vps34-Vps15 complex, which is crucial for autophagy. Beclin 1 also interacts with anti-apoptotic proteins like Bcl-2 and Bcl-XL, but its interaction can be disrupted by phosphorylation or ubiquitination. Caspase-mediated cleavage of Beclin 1 promotes crosstalk between apoptosis and autophagy. Beclin 1 dysfunction is implicated in various disorders, including cancer and neurodegeneration. The review highlights the organization and function of the Beclin 1 network, focusing on the cross-regulation between apoptosis and autophagy. Key findings include the involvement of transcription factors (NF-κB, E2F) and microRNAs in Beclin 1 regulation, as well as the roles of specific Beclin 1-binding proteins such as Atg14L, UVRAG, Bif-1, Rubicon, Ambr1, HMGB1, nPIST, VMP1, SLAM, IP3R, PINK1, and survivin. The review also discusses the complex interactions between Beclin 1 and its binding partners, and the dynamic regulation of these interactions by phosphorylation and ubiquitination. Finally, it explores the crosstalk between apoptosis and autophagy, emphasizing the mutual inhibition and regulatory mechanisms involving Beclin 1.The Beclin 1 network plays a central role in regulating autophagy, a process essential for cellular homeostasis. Beclin 1, the mammalian orthologue of yeast Atg6, interacts with various cofactors to form core complexes that promote autophagosome formation and maturation. These complexes include the Beclin 1-Vps34-Vps15 complex, which is crucial for autophagy. Beclin 1 also interacts with anti-apoptotic proteins like Bcl-2 and Bcl-XL, but its interaction can be disrupted by phosphorylation or ubiquitination. Caspase-mediated cleavage of Beclin 1 promotes crosstalk between apoptosis and autophagy. Beclin 1 dysfunction is implicated in various disorders, including cancer and neurodegeneration. The review highlights the organization and function of the Beclin 1 network, focusing on the cross-regulation between apoptosis and autophagy. Key findings include the involvement of transcription factors (NF-κB, E2F) and microRNAs in Beclin 1 regulation, as well as the roles of specific Beclin 1-binding proteins such as Atg14L, UVRAG, Bif-1, Rubicon, Ambr1, HMGB1, nPIST, VMP1, SLAM, IP3R, PINK1, and survivin. The review also discusses the complex interactions between Beclin 1 and its binding partners, and the dynamic regulation of these interactions by phosphorylation and ubiquitination. Finally, it explores the crosstalk between apoptosis and autophagy, emphasizing the mutual inhibition and regulatory mechanisms involving Beclin 1.