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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
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pubmed:dateCreated |
1998-6-12
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pubmed:abstractText |
Adenovirus E1B-19K and BCL-2 anti-apoptosis proteins interact with certain BCL-2 family pro-apoptotic proteins. A conserved domain, BH3, present in these proteins is essential for their pro-apoptotic activity and for heterodimerization with anti-apoptosis proteins. Cellular protein BNIP3 (previously NIP3) interacts with E1B-19K, BCL-2, BCL-xL, and EBV-BHRF1. BNIP3 contains a motif similar to the BH3 domain. Deletion of the BH3-like motif in BNIP3 abrogates its ability to heterodimerize with E1B-19K and BCL-xL. Substitution of the BH3 domain of BNIP3 for the corresponding sequences of BAX functionally restores the pro-apoptotic and protein heterodimerization activities of BAX. BNIP3 exhibits a delayed cell death activity that is partially relieved by deletion of the BH3 domain. BNIP3 suppresses the anti-apoptosis activity of BCL-xL in a BH3-dependent manner. BNIP3 contains a C-terminal trans-membrane (TM) domain similar to other BCL-2 family proteins and BNIP1 (previously NIP1). The TM domains of BNIP3 and BNIP1 can functionally substitute for the TM domain of a BCL-2 family member EBV-BHRF1. The BNIP3 TM domain exclusively targets the heterologous green fluorescent protein (GFP) to mitochondria. These results suggest that BNIP3 is a member of the BH3-contaning BCL-2 family of pro-apoptotic proteins and functions in mitochondria.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenovirus E1B Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/BNIP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BNIP3L protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-2-Associated X Protein
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
273
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
12415-21
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9575197-Adenovirus E1B Proteins,
pubmed-meshheading:9575197-Amino Acid Sequence,
pubmed-meshheading:9575197-Animals,
pubmed-meshheading:9575197-Apoptosis,
pubmed-meshheading:9575197-COS Cells,
pubmed-meshheading:9575197-Membrane Proteins,
pubmed-meshheading:9575197-Mitochondria,
pubmed-meshheading:9575197-Molecular Sequence Data,
pubmed-meshheading:9575197-Proto-Oncogene Proteins,
pubmed-meshheading:9575197-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:9575197-Sequence Deletion,
pubmed-meshheading:9575197-Subcellular Fractions,
pubmed-meshheading:9575197-Tumor Suppressor Proteins,
pubmed-meshheading:9575197-bcl-2-Associated X Protein
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pubmed:year |
1998
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pubmed:articleTitle |
Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence.
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pubmed:affiliation |
Institute for Molecular Virology, St. Louis University Medical Center, St. Louis, Missouri 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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