Premium
Limited caspase cleavage of human BAP31
Author(s) -
Määttä Juha,
Hallikas Outi,
Welti Saara,
Hildén Pekka,
Schröder Jim,
Kuismanen Esa
Publication year - 2000
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/s0014-5793(00)02159-1
Subject(s) - cycloheximide , staurosporine , cleavage (geology) , endoplasmic reticulum , golgi apparatus , microbiology and biotechnology , chemistry , tunicamycin , apoptosis , cleavage and polyadenylation specificity factor , caspase , cleavage stimulation factor , cleavage factor , biology , biochemistry , protein biosynthesis , programmed cell death , unfolded protein response , enzyme , messenger rna , paleontology , protein kinase c , polyadenylation , fracture (geology) , gene
Human BAP31 was cleaved at both of its two identical caspase cleavage sites in two previously reported models of apoptosis. We show here that only the most carboxy‐terminal site is cleaved during apoptosis induced in HeLa cells by tunicamycin, tumor necrosis factor and cycloheximide, or staurosporine. Similar results were obtained in HL‐60 cells using Fas/APO‐1 antibodies, or cycloheximide. This limited cleavage, which is inhibited by several caspase inhibitors, removes eight amino acids from human BAP31 including the KKXX coat protein I binding motif. Ectopic expression of the resulting cleavage product induces redistribution of mannosidase II from the Golgi and prevents endoplasmic reticulum to Golgi transport of virus glycoproteins.