Limited caspase cleavage of human BAP31

被引:21
作者
Määttä, J
Hallikas, O
Welti, S
Hildén, P
Schroder, J
Kuismanen, E
机构
[1] Univ Helsinki, Viikki Bioctr, Div Biochem, Dept Biosci, Helsinki 00014, Finland
[2] Univ Helsinki, Viikki Bioctr, Div Genet, Dept Biosci, Helsinki 00014, Finland
来源
FEBS LETTERS | 2000年 / 484卷 / 03期
基金
芬兰科学院;
关键词
apoptosis; BAP31; caspase cleavage; endoplasmic reticulum; Golgi apparatus;
D O I
10.1016/S0014-5793(00)02159-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V, All rights reserved.
引用
收藏
页码:202 / 206
页数:5
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