Article
Endoproteolytic cleavage of its propeptide is a prerequisite for efficient transport of furin out of the endoplasmic reticulum.
The Journal of biological chemistry - 10 Feb 1995
Creemers J W, Vey M, Schäfer W, Ayoubi T A, Roebroek A J, Klenk H D, Garten W, Van de Ven W J
Abstract excerpt
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...
Topics
- Amino Acid Sequence
- Animals
- Base Sequence
- Binding Sites
- Biological Transport
- Cattle
- Cell Line
- DNA Primers
- Endoplasmic Reticulum
- Furin
- Glycosylation
- Humans
- Hydrolysis
- Molecular Sequence Data
- Mutation
- Peptides
- Protein Precursors
- Protein Processing, Post-Translational