Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Antibodies, Monoclonal / pharmacology
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Apoptosis / drug effects
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Apoptosis / physiology
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Binding Sites
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Caspases / metabolism*
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Cycloheximide / pharmacology
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Endoplasmic Reticulum / metabolism
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Golgi Apparatus / metabolism
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HeLa Cells
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Humans
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Mannosidases / metabolism
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Membrane Proteins*
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Mice
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Mice, Inbred BALB C
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Protein Transport
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Proteins / metabolism*
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Recombinant Fusion Proteins / metabolism
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Staurosporine / pharmacology
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Transfection
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Tumor Necrosis Factor-alpha / pharmacology
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Tunicamycin / pharmacology
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fas Receptor / immunology
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fas Receptor / physiology
Substances
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Antibodies, Monoclonal
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BCAP31 protein, human
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Bcap31 protein, mouse
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Membrane Proteins
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Proteins
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Recombinant Fusion Proteins
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Tumor Necrosis Factor-alpha
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fas Receptor
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Tunicamycin
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Cycloheximide
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Mannosidases
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mannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidase
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Caspases
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Staurosporine