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Biologically active APRIL is secreted following intracellular processing in the Golgi apparatus by furin convertase
Author(s) -
LópezFraga M,
Fernández R,
Albar J P,
Hahne M
Publication year - 2001
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kve198
Subject(s) - furin , brefeldin a , golgi apparatus , endoplasmic reticulum , secretion , microbiology and biotechnology , b cell activating factor , secretory pathway , biology , intracellular , transmembrane protein , endosome , receptor , secretory protein , cell surface receptor , biochemistry , b cell , antibody , immunology , enzyme
Tumor necrosis factor (TNF) ligand family members are synthesized as transmembrane proteins, and cleavage of the membrane‐anchored proteins from the cell surface is frequently observed. The TNF‐related ligands APRIL and BLyS and their cognate receptors BCMA/TACI form a two ligand/two receptor system that has been shown to participate in B‐ and T‐cell stimulation. In contrast to BLyS, which is known to be cleaved from the cell surface, we found that APRIL is processed intracellularly by furin convertase. Blockage of protein transport from the endoplasmic reticulum to the Golgi apparatus by Brefeldin A treatment abrogated APRIL processing, whereas monensin, an inhibitor of post‐Golgi transport, did not interfere with cleavage of APRIL, but blocked secretion of processed APRIL. Thus, APRIL shows a unique maturation pathway among the TNF ligand family members, as it not detectable as a membrane‐anchored protein at the cell surface, but is processed in the Golgi apparatus prior to its secretion.