Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis
Caspase 8 plays an essential role in the execution of death receptor-mediated apoptosis. To determine the localization of endogenous caspase 8, we used a panel of subunit-specific anti-caspase 8 monoclonal antibodies in confocal immunofluorescence microscopy. In the human breast carcinoma cell line...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
August 1, 2000
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| In: |
Molecular and cellular biology
Year: 2000, Volume: 20, Issue: 15, Pages: 5665-5679 |
| ISSN: | 1098-5549 |
| DOI: | 10.1128/MCB.20.15.5665-5679.2000 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1128/MCB.20.15.5665-5679.2000 Verlag, lizenzpflichtig, Volltext: https://mcb.asm.org/content/20/15/5665 
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| Author Notes: | Alexander H. Stegh, Harald Herrmann, Stefan Lampel, Dieter Weisenberger, Kerstin Andrä, Martin Seper, Gerhard Wiche, Peter H. Krammer, and Marcus E. Peter |
MARC
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| 520 | |a Caspase 8 plays an essential role in the execution of death receptor-mediated apoptosis. To determine the localization of endogenous caspase 8, we used a panel of subunit-specific anti-caspase 8 monoclonal antibodies in confocal immunofluorescence microscopy. In the human breast carcinoma cell line MCF7, caspase 8 predominantly colocalized with and bound to mitochondria. After induction of apoptosis through CD95 or tumor necrosis factor receptor I, active caspase 8 translocated to plectin, a major cross-linking protein of the three main cytoplasmic filament systems, whereas the caspase 8 prodomain remained bound to mitochondria. Plectin was quantitatively cleaved by caspase 8 at Asp 2395 in the center of the molecule in all cells tested. Cleavage of plectin clearly preceded that of other caspase substrates such as poly(ADP-ribose) polymerase, gelsolin, cytokeratins, or lamin B. In primary fibroblasts from plectin-deficient mice, apoptosis-induced reorganization of the actin cytoskeleton, as seen in wild-type cells, was severely impaired, suggesting that during apoptosis, plectin is required for the reorganization of the microfilament system. | ||
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