|Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.|
|PMID: 12198154 Owner: NLM Status: MEDLINE|
|The involvement of the death adaptor protein FADD and the apoptosis-initiating caspase-8 in CD95 and TRAIL death signalling has recently been demonstrated by the analysis of the native death-inducing signalling complex (DISC) that forms upon ligand-induced receptor cross-linking. However, the role of caspase-10, the other death-effector-domain-containing caspase besides caspase-8, in death receptor signalling has been controversial. Here we show that caspase-10 is recruited not only to the native TRAIL DISC but also to the native CD95 DISC, and that FADD is necessary for its recruitment to and activation at these two protein complexes. With respect to the function of caspase-10, we show that it is not required for apoptosis induction. In addition, caspase-10 can not substitute for caspase-8, as the defect in apoptosis induction observed in caspase-8-deficient cells could not be rescued by overexpression of caspase-10. Finally, we demonstrate that caspase-10 is cleaved during CD95-induced apoptosis of activated T cells. These results show that caspase-10 activation occurs in primary cells, but that its function differs from that of caspase-8.|
|Martin R Sprick; Eva Rieser; Heiko Stahl; Anne Grosse-Wilde; Markus A Weigand; Henning Walczak|
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|Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't|
|Title: The EMBO journal Volume: 21 ISSN: 0261-4189 ISO Abbreviation: EMBO J. Publication Date: 2002 Sep|
|Created Date: 2002-08-28 Completed Date: 2002-10-08 Revised Date: 2009-11-18|
Medline Journal Info:
|Nlm Unique ID: 8208664 Medline TA: EMBO J Country: England|
|Languages: eng Pagination: 4520-30 Citation Subset: IM|
|Division for Apoptosis Regulation, Tumour Immunology Program, DKFZ, Heidelberg, Germany.|
|APA/MLA Format Download EndNote Download BibTex|
Adaptor Proteins, Signal Transducing*
Antigens, CD95 / physiology*
Apoptosis / physiology*
Apoptosis Regulatory Proteins
B-Lymphocytes / metabolism
Carrier Proteins / physiology*
Caspases / metabolism, physiology*
Fas-Associated Death Domain Protein
Jurkat Cells / metabolism
Membrane Glycoproteins / physiology*
Protein Isoforms / physiology
Protein Structure, Tertiary
Receptors, TNF-Related Apoptosis-Inducing Ligand
Receptors, Tumor Necrosis Factor / genetics, metabolism
T-Lymphocytes / metabolism
TNF-Related Apoptosis-Inducing Ligand
Tumor Necrosis Factor-alpha / physiology*
|0/Adaptor Proteins, Signal Transducing; 0/Antigens, CD95; 0/Apoptosis Regulatory Proteins; 0/CASP10 protein, human; 0/Carrier Proteins; 0/FADD protein, human; 0/Fas-Associated Death Domain Protein; 0/Macromolecular Substances; 0/Membrane Glycoproteins; 0/Protein Isoforms; 0/Receptors, TNF-Related Apoptosis-Inducing Ligand; 0/Receptors, Tumor Necrosis Factor; 0/TNF-Related Apoptosis-Inducing Ligand; 0/TNFRSF10A protein, human; 0/TNFRSF10B protein, human; 0/TNFSF10 protein, human; 0/Tumor Necrosis Factor-alpha; EC 3.4.22.-/CASP8 protein, human; EC 3.4.22.-/CASP9 protein, human; EC 3.4.22.-/Caspase 10; EC 3.4.22.-/Caspase 8; EC 3.4.22.-/Caspase 9; EC 3.4.22.-/Caspases|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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