Acidic leucine-rich nuclear phosphoprotein 32 family member E (ANP32E)

Acidic leucine-rich nuclear phosphoprotein 32 family member E (ANP32E) is a small, evolutionarily conserved nuclear protein characterized by an N-terminal leucine-rich repeat domain and a C-terminal acidic region[2][5]. Its principal function is as a histone chaperone, particularly for H2A.Z, facilitating the removal of H2A.Z from chromatin and stabilizing the H2A.Z-H2B dimer in the cytoplasm and nucleoplasm[1][3][4][6]. Unlike classical chromatin remodelers, ANP32E is not a stable component of major chromatin remodeling complexes but acts to buffer and stabilize soluble H2A.Z in a cell cycle-dependent manner, ensuring proper nuclear import and chromatin incorporation of H2A.Z[3][4]. ANP32E also inhibits protein phosphatase 2A (PP2A) activity and may participate in apoptotic regulation and intracellular transport pathways[2][6]. Dysregulation of ANP32E has been implicated in cancer cell proliferation, with context-dependent roles that may be oncogenic[3][5]. No drugs, biomarkers, or safety data are currently documented for direct targeting of ANP32E as a therapeutic target.

Other names

Acidic nuclear phosphoprotein 32 family member EANP32EAcidic leucine-rich nuclear phosphoprotein 32 family member ELANP-LLANPLMGC5350LANP-like proteinLeucine-rich acidic nuclear protein like