Processing of protein precursors by a novel family of subtilisin-related mammalian endoproteases.
The recent identification of a novel family of mammalian endoproteases that carry out intracellular processing of protein precursors at dibasic sites has ended a search that began twenty-five years ago with the discovery of the first such precursor, proinsulin. The five proteases found thus far are all related to the yeast dibasic-specific endoprotease kex2, and include PC2, PC3/PC1, PC4, furin/PACE, and PACE4. All are Ca(2+)-dependent serine proteases with catalytic domains organized similarly to the bacterial subtilisins. The emerging characteristics of these endoproteases, including their tissue-specific expression, subcellular localization, and cleavage site selectivity, indicates that members of this family arose during evolution to process a diverse group of functionally distinct precursors in a highly specific, compartmentalized and regulated fashion.
Smeekens
S P
SP
Chiron Corporation, Emeryville, CA 94608.
D000595:Amino Acid Sequence; D000818:Animals; D010450:Endopeptidases / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D013381:Subtilisins / Q000378:metabolism
D011498:Protein Precursors; D010450:Endopeptidases; D013381:Subtilisins