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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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Hauptverfasser: Stegh, Alexander H. (VerfasserIn) , Krammer, Peter H. (VerfasserIn) , Peter, Marcus E. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: August 1, 2000
In: Molecular and cellular biology
Year: 2000, Jahrgang: 20, Heft: 15, Pages: 5665-5679
ISSN:1098-5549
DOI:10.1128/MCB.20.15.5665-5679.2000
Online-Zugang: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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Verfasserangaben:Alexander H. Stegh, Harald Herrmann, Stefan Lampel, Dieter Weisenberger, Kerstin Andrä, Martin Seper, Gerhard Wiche, Peter H. Krammer, and Marcus E. Peter
Beschreibung
Zusammenfassung: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.
Beschreibung:Gesehen am 26.04.2021
Beschreibung:Online Resource
ISSN:1098-5549
DOI:10.1128/MCB.20.15.5665-5679.2000

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