Bcl-2-like protein 2–poly(A) binding protein nuclear 1 fusion protein (BCL2L2-PABPN1)

BCL2L2-PABPN1 is a fusion protein derived from read-through transcription involving BCL2L2 (encoding the anti-apoptotic regulator BCL-W) and PABPN1 (an RNA binding protein crucial for nuclear polyadenylation). The BCL2L2 portion antagonizes mitochondrial apoptotic pathways by sequestering pro-apoptotic BH3-only proteins and inhibiting the activation of effectors like Bax and Bak. BCL-W contributes to tumor cell survival, chemoresistance, and suppression of apoptosis, particularly in cancer types where its expression is upregulated. The fusion may also result in altered subcellular localization or regulatory function, due to incorporation of RNA-related properties from PABPN1, with possible effects on RNA metabolism. This chimeric molecule is increasingly recognized as relevant for oncogenesis, especially regarding apoptosis resistance and disease progression in multiple cancer types (lung, prostate, glioma, etc.). Associated roles also extend to normal physiological regulation of cell survival in certain tissues (endothelium, hematopoietic lineages), and rare muscular disorders.

Other names

BCL2L2-PABPN1 readthroughBCL2L2BCLWKIAA0271Bcl2-L-2Apoptosis regulator Bcl-WBCL2L2-PABPN1 protein

Inhibition of anti-apoptotic BCL2L2/BCL-W function, promoting pro-apoptotic signaling and mitochondrial outer membrane permeabilization. Potential modulation of RNA processing and stability (if fusion leads to functional alterations).