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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
39
|
| pubmed:dateCreated |
1996-11-18
|
| pubmed:abstractText |
Adenovirus E1B 19-kDa protein (19K) is a member of the Bcl-2 family of suppressors of apoptosis. The suppressors function through heterodimerization with the death promoters, Bax and related proteins, thus establishing a set point within the cell that determines whether or not apoptosis is executed in response to a death signal. Sequence similarities between 19K and Bcl-2 are largely restricted to short Bcl-2 homology (BH) domains that mediate interaction with Bax. The BH1 sequence in 19K is degenerate but nevertheless contains a conserved glycine residue found in all family members that when mutated to alanine in Bcl-2 results in loss of Bcl-2 function and ability to dimerize with Bax (Yin, X.-M., Oltvai, Z. N., and Korsmeyer, S. J. (1994) Nature 369, 321-323). Here, we show that the analogous mutation in BH1 of 19K also abrogates the anti-apoptotic properties of 19K and its ability to interact with Bax, thus establishing the critical importance of this residue within BH1 and the likely similarity of Bcl-2 and 19K function. In distinct contrast to Bcl-2, however, 19K interaction was not detected with Bad, a Bcl-2/Bcl-XL dimerizing protein that can potentially regulate a Bax middle dotBcl-2/Bcl-XL survival set point and reinstate susceptibility to a death signal. Furthermore, the anti-apoptotic function of 19K was not overcome by enforced expression of Bad in transfected cells. This feature of 19K may provide adenovirus with a selective advantage in evading premature induction of apoptosis by the host cell.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenovirus E1B Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/BAD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BAX protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bad protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Bax protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier 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/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-2-Associated X Protein,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-Associated Death Protein
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
27
|
| pubmed:volume |
271
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
24221-5
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8798665-Adenovirus E1B Proteins,
pubmed-meshheading:8798665-Adenoviruses, Human,
pubmed-meshheading:8798665-Animals,
pubmed-meshheading:8798665-Apoptosis,
pubmed-meshheading:8798665-Binding Sites,
pubmed-meshheading:8798665-CHO Cells,
pubmed-meshheading:8798665-Carrier Proteins,
pubmed-meshheading:8798665-Cricetinae,
pubmed-meshheading:8798665-Humans,
pubmed-meshheading:8798665-Mice,
pubmed-meshheading:8798665-Protein Binding,
pubmed-meshheading:8798665-Proto-Oncogene Proteins,
pubmed-meshheading:8798665-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:8798665-Recombinant Proteins,
pubmed-meshheading:8798665-bcl-2-Associated X Protein,
pubmed-meshheading:8798665-bcl-Associated Death Protein
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Adenovirus E1B 19-kDa death suppressor protein interacts with Bax but not with Bad.
|
| pubmed:affiliation |
Department of Biochemistry, McIntyre Medical Sciences Building, McGill University, Montreal, Quebec, Canada H3G 1Y6.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|