Limited caspase cleavage of human BAP31

Juha Maatta, Outi Hallikas, Saara Welti, Pekka Hilden, Jim Schöder, Esa Kuismanen

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

Sammanfattning

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.
Originalspråkengelska
TidskriftFEBS Letters
Volym484
Utgåva3
Sidor (från-till)202-206
Antal sidor5
ISSN0014-5793
StatusPublicerad - 10 nov. 2000
MoE-publikationstypA1 Tidskriftsartikel-refererad

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