A predicted alpha -helix mediates targeting of the proprotein convertase PC1 to the regulated secretory pathway.
The proprotein convertase PC1 is a protease whose activity is largely confined to the dense core secretory granules of neuroendocrine cells. Efficient processing of PC1 substrates in granules requires a mechanism that will both limit the activity of the enzyme to these organelles and promote its targeting to the nascent secretory granules. In the current study, we provide evidence that targeting of PC1 to secretory granules is mediated by alpha-helical structures in its C-terminal tail and, at least in part, is dependent on interactions with specific components of the secretory granule membrane.
Jutras
I
I
Laboratories of Molecular Biochemistry of Hypertension and Biochemical Neuroendocrinology, Clinical Research Institute of Montreal, Montreal, Quebec H2W 1R7, Canada.
Seidah
N G
NG
Reudelhuber
T L
TL
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D001483:Base Sequence; D002460:Cell Line; D017931:DNA Primers; D008969:Molecular Sequence Data; D043484:Proprotein Convertases; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism
D017931:DNA Primers; D011993:Recombinant Fusion Proteins; D043484:Proprotein Convertases; D016282:Aspartic Acid Endopeptidases