Mitochondrial-processing peptidase subunit alpha (PMPCA)

Mitochondrial-processing peptidase subunit alpha (PMPCA) is the alpha subunit of mitochondrial processing peptidase (MPP), a heterodimeric enzyme located in the mitochondrial matrix that is essential for cleaving the N-terminal transit peptides from nuclear-encoded mitochondrial precursor proteins, thereby enabling their proper folding, import, and maturation[1][2][4]. It forms a functional heterodimer with the beta subunit (PMPCB), which contains the catalytic site, while PMPCA is necessary for substrate recognition and binding[1][2]. Deficiency or mutation in PMPCA impairs mitochondrial protein processing, and is causally linked to a range of neurodegenerative diseases, including autosomal recessive spinocerebellar ataxia and Friedreich ataxia, as well as late-onset dominant optic atrophy[3][4]. PMPCA’s activity is indispensable for cellular viability, especially neuronal health, and altering its function can cause severe mitochondrial dysfunction and neurodegeneration[1][2][3][4].

Other names

Alpha-MPPP-55Inactive zinc metalloprotease alphaMAS2INPP5EMPPACerebellar ataxia-1Spinocerebellar ataxia, autosomal recessive 2CLA1SCAR2KIAA0123CPD3Peptidase (mitochondrial processing) alpha