rdf:type |
|
lifeskim:mentions |
umls-concept:C0023418,
umls-concept:C0023688,
umls-concept:C0039194,
umls-concept:C0162638,
umls-concept:C0205263,
umls-concept:C0205369,
umls-concept:C0291573,
umls-concept:C0333516,
umls-concept:C0385242,
umls-concept:C0596311,
umls-concept:C1330957,
umls-concept:C1336646,
umls-concept:C1366587
|
pubmed:issue |
11
|
pubmed:dateCreated |
2005-3-14
|
pubmed:abstractText |
Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces programmed cell death through the caspase activation cascade and translocation of cleaved Bid (tBid) by the apical caspase-8 to mitochondria to induce oligomerization of multidomain Bax and Bak. However, the roles of prosurvival Bcl-2 family proteins in TRAIL apoptosis remain elusive. Here we showed that, besides the specific cleavage and activation of Bid by caspase-8 and caspase-3, TRAIL-induced apoptosis in Jurkat T cells required the specific cleavage of Mcl-1 at Asp-127 and Asp-157 by caspase-3, while other prototypic antiapoptotic factors such as Bcl-2 or Bcl-X(L) seemed not to be affected. Mutation at Asp-127 and Asp-157 of Mcl-1 led to cellular resistance to TRAIL-induced apoptosis. In sharp contrast to cycloheximide-induced Mcl-1 dilapidation, TRAIL did not activate proteasomal degradation of Mcl-1 in Jurkat cells. We further established for the first time that the C-terminal domain of Mcl-1 became proapoptotic as a result of caspase-3 cleavage, and its physical interaction and cooperation with tBid, Bak, and voltage-dependent anion-selective channel 1 promoted mitochondrial apoptosis. These results suggested that removal of N-terminal domains of Bid by caspase-8 and Mcl-1 by caspase-3 enabled the maximal mitochondrial perturbation that potentiated TRAIL-induced apoptosis.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apoptosis Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/BCL2L1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BH3 Interacting Domain Death...,
http://linkedlifedata.com/resource/pubmed/chemical/BID protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bcl2l1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Bid protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Casp3 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Casp8 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 8,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cycloheximide,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes c,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Synthesis Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/TNF-Related Apoptosis-Inducing...,
http://linkedlifedata.com/resource/pubmed/chemical/TNFSF10 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tnfsf10 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-X Protein,
http://linkedlifedata.com/resource/pubmed/chemical/myeloid cell leukemia sequence 1...
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
|
pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
18
|
pubmed:volume |
280
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
10491-500
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pubmed:dateRevised |
2008-7-9
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pubmed:meshHeading |
pubmed-meshheading:15637055-Amino Acid Sequence,
pubmed-meshheading:15637055-Animals,
pubmed-meshheading:15637055-Apoptosis,
pubmed-meshheading:15637055-Apoptosis Regulatory Proteins,
pubmed-meshheading:15637055-Aspartic Acid,
pubmed-meshheading:15637055-BH3 Interacting Domain Death Agonist Protein,
pubmed-meshheading:15637055-Binding Sites,
pubmed-meshheading:15637055-Carrier Proteins,
pubmed-meshheading:15637055-Caspase 3,
pubmed-meshheading:15637055-Caspase 8,
pubmed-meshheading:15637055-Caspases,
pubmed-meshheading:15637055-Cell Death,
pubmed-meshheading:15637055-Cell Line, Tumor,
pubmed-meshheading:15637055-Cell Survival,
pubmed-meshheading:15637055-Cycloheximide,
pubmed-meshheading:15637055-Cytochromes c,
pubmed-meshheading:15637055-Down-Regulation,
pubmed-meshheading:15637055-Glutathione Transferase,
pubmed-meshheading:15637055-HeLa Cells,
pubmed-meshheading:15637055-Humans,
pubmed-meshheading:15637055-Immunoprecipitation,
pubmed-meshheading:15637055-Jurkat Cells,
pubmed-meshheading:15637055-Leukemia,
pubmed-meshheading:15637055-Membrane Glycoproteins,
pubmed-meshheading:15637055-Microscopy, Fluorescence,
pubmed-meshheading:15637055-Mitochondria,
pubmed-meshheading:15637055-Molecular Sequence Data,
pubmed-meshheading:15637055-Mutagenesis, Site-Directed,
pubmed-meshheading:15637055-Mutation,
pubmed-meshheading:15637055-Neoplasm Proteins,
pubmed-meshheading:15637055-Plasmids,
pubmed-meshheading:15637055-Point Mutation,
pubmed-meshheading:15637055-Proteasome Endopeptidase Complex,
pubmed-meshheading:15637055-Protein Structure, Tertiary,
pubmed-meshheading:15637055-Protein Synthesis Inhibitors,
pubmed-meshheading:15637055-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:15637055-RNA, Messenger,
pubmed-meshheading:15637055-RNA, Small Interfering,
pubmed-meshheading:15637055-Rats,
pubmed-meshheading:15637055-Reticulocytes,
pubmed-meshheading:15637055-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:15637055-TNF-Related Apoptosis-Inducing Ligand,
pubmed-meshheading:15637055-Tumor Necrosis Factor-alpha,
pubmed-meshheading:15637055-bcl-X Protein
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pubmed:year |
2005
|
pubmed:articleTitle |
Specific cleavage of Mcl-1 by caspase-3 in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in Jurkat leukemia T cells.
|
pubmed:affiliation |
Center for Molecular Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China 100080.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|