Nascent polypeptide-associated complex subunit alpha (NACA)

Nascent polypeptide-associated complex subunit alpha (NACA) is the alpha subunit of the nascent polypeptide-associated complex (NAC), a highly conserved chaperone that binds nascent polypeptides as they emerge from ribosomes in eukaryotic cells and prevents inappropriate protein-protein interactions and mistargeting to the endoplasmic reticulum[1][3][5]. NACA forms a heterodimer with BTF3 (beta subunit), and together, the complex modulates protein sorting, assists in folding, and protects against aggregation. Apart from its canonical role as a ribosome-bound chaperone, NACA is also a transcription coactivator—regulating gene expression during muscle, bone, and erythroid development, mediating tissue-specific differentiation, and modulating anti-apoptotic signaling[3][5]. NACA and its muscle-specific isoform (skNAC) are required for normal muscle and bone development and are implicated in controlling the proliferation and differentiation of several cell types. Aberrant NACA expression or function is linked to cancer progression, certain neurodegenerative diseases, and acts as an IgE autoantigen in atopic dermatitis[3][5]. No drugs are currently approved that specifically target NACA, and its essential cellular roles suggest that direct inhibition may pose safety concerns.

Other names

HSD48NAC-alphaNACA1SKNACAlpha-NACMuscle-specific form (skNAC)Nascent-polypeptide-associated complex alpha polypeptide

Not applicable / no known approved drugs specifically targeting this molecule