[HTML][HTML] The Ordered and Compartment-specific Autoproteolytic Removal of the Furin Intramolecular Chaperone Is Required for Enzyme Activation∗
ED Anderson, SS Molloy, F Jean, H Fei… - Journal of Biological …, 2002 - ASBMB
The propeptide of furin has multiple roles in guiding the activation of the endoprotease in
vivo. The 83-residue N-terminal propeptide is autoproteolytically excised in the endoplasmic
reticulum (ER) at the consensus furin site,-Arg 104-Thr-Lys-Arg 107↓-, but remains bound
to furin as a potent autoinhibitor. Furin lacking the propeptide is ER-retained and
proteolytically inactive. Co-expression with the propeptide, however, restores trans-Golgi
network (TGN) localization and enzyme activity, indicating that the furin propeptide is an …
vivo. The 83-residue N-terminal propeptide is autoproteolytically excised in the endoplasmic
reticulum (ER) at the consensus furin site,-Arg 104-Thr-Lys-Arg 107↓-, but remains bound
to furin as a potent autoinhibitor. Furin lacking the propeptide is ER-retained and
proteolytically inactive. Co-expression with the propeptide, however, restores trans-Golgi
network (TGN) localization and enzyme activity, indicating that the furin propeptide is an …