[HTML][HTML] Endoproteolytic Cleavage of Its Propeptide Is a Prerequisite for Efficient Transport of Furin Out of the Endoplasmic Reticulum (∗)
JWM Creemers, M Vey, W Schäfer, TAY Ayoubi… - Journal of Biological …, 1995 - ASBMB
The trans-Golgi network (TGN) proprotein convertase furin is synthesized in a zymogenic
form and is activated by intramolecular, autoproteolytic cleavage of the propeptide from its
precursor. To obtain insight in possible functions of the furin propeptide, we have studied
biosynthesis, propeptide cleavage, biological activity, and intracellular localization of human
and bovine furin. Analysis of autocatalytic cleavage site mutants of furin revealed that
efficient propeptide cleavage requires the presence of the complete furin cleavage …
form and is activated by intramolecular, autoproteolytic cleavage of the propeptide from its
precursor. To obtain insight in possible functions of the furin propeptide, we have studied
biosynthesis, propeptide cleavage, biological activity, and intracellular localization of human
and bovine furin. Analysis of autocatalytic cleavage site mutants of furin revealed that
efficient propeptide cleavage requires the presence of the complete furin cleavage …