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Evidence for proprotein convertase activity in the endoplasmic reticulum/early Golgi
Author(s) -
Salvas Alexandre,
Benjannet Suzanne,
Reudelhuber Timothy L.,
Chrétien Michel,
Seidah Nabil G.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.09.029
Subject(s) - proprotein convertases , endoplasmic reticulum , furin , golgi apparatus , proprotein convertase , subtilisin , chemistry , secretory pathway , microbiology and biotechnology , zymogen , biochemistry , prohormone convertase , biology , enzyme , prohormone , hormone , lipoprotein , ldl receptor , cholesterol
Processing of precursor proteins by the proprotein convertases is thought to occur mainly in the trans ‐Golgi network or post‐Golgi compartments. Such cleavage is inhibited by the prosegment of the convertases. During our studies of the use of the inhibitory prosegment of PC1, we noticed that a construct containing the prosegment fused to the C‐terminal secretory granule sorting domain was cleaved in the endoplasmic reticulum (ER) at a pair of basic residues, best recognized by furin and PC7. This was further confirmed when this construct was fused at the C‐terminus with a KDEL ER‐retention signal. This suggests that the convertases could cleave some substrates within the ER, possibly by displacing the inhibitory prosegment associated with them.