Lon peptidase 2, peroxisomal (LONP2)

Lon peptidase 2, peroxisomal (LONP2) is an ATP-dependent serine protease localized to the peroxisomal matrix, where it plays a fundamental role in peroxisomal protein quality control by degrading misfolded, oxidized, or unassembled proteins[1][3]. LONP2 is structurally characterized by an N-terminal substrate recognition domain (Lon N), a central ATPase (AAA+) domain, and a C-terminal proteolytic domain, with a peroxisomal targeting signal at its C-terminus that directs it into peroxisomes[1][2][3]. Expressed throughout the body with highest levels in pancreas, liver, and kidney, LONP2 is essential for maintaining peroxisome function—particularly in removing dysfunctional matrix proteins damaged by high concentrations of reactive oxygen species produced during fatty acid β-oxidation and other peroxisomal oxidative processes[1][2][3][5]. In addition to protease activity, LONP2 displays chaperone-like functions, assisting in protein folding during peroxisome biogenesis and protein import. Loss or malfunction of LONP2 disrupts peroxisome homeostasis, potentially contributing to disease, aging, or cancer[1][3][4]. No drugs currently target LONP2 directly, but its central role in proteostasis makes it a subject of ongoing research.

Other names

Lon protease homolog 2Peroxisomal Lon proteaseLONPLONPLLon protease 2pLonMGC4840PLONPSLONlon protease-like protein 2peroxisomal Lon protease homolog 2

Null (no known marketed or investigated drug mechanisms targeting LONP2 directly)