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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1989-3-17
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pubmed:abstractText |
The BNLF-1 gene from Epstein-Barr virus (EBV) induces anchorage-independent and tumorigenic growth in rodent cell lines. The BNLF-1 protein (also termed LMP) is a membrane protein, and its predicted amino acid sequence indicates that the protein has six membrane-spanning segments in addition to a short amino-terminal (approximately 25 amino acids) and a long carboxyl-terminal (approximately 200 amino acids) cytoplasmic domain. To identify the regions of the protein that are essential for its transforming activity, we have constructed deletion mutants of the BNLF-1 gene and tested them for transforming activity. Surprisingly, the entire carboxyl-terminal cytoplasmic domain is dispensable for transforming activity, whereas the putative membrane-spanning segments are essential. These observations indicate that BNLF-1 has a novel function that is distinct from the functions associated with other membrane-associated viral transforming proteins. We speculate that BNLF-1 is a receptor for a growth-promoting agent, with its trans-membrane domain involved in ligand binding, and its amino-terminal domain or cytoplasmic loops involved in coupling BNLF-1 to effector molecules in the cell, a situation analogous to the rhodopsin group of receptors.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0950-9232
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
67-74
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2536919-Amino Acid Sequence,
pubmed-meshheading:2536919-Animals,
pubmed-meshheading:2536919-Cell Adhesion,
pubmed-meshheading:2536919-Cell Division,
pubmed-meshheading:2536919-Cell Fractionation,
pubmed-meshheading:2536919-Cell Line,
pubmed-meshheading:2536919-Cell Transformation, Neoplastic,
pubmed-meshheading:2536919-Cell Transformation, Viral,
pubmed-meshheading:2536919-Herpesvirus 4, Human,
pubmed-meshheading:2536919-Immunoblotting,
pubmed-meshheading:2536919-Membrane Proteins,
pubmed-meshheading:2536919-Mice,
pubmed-meshheading:2536919-Mice, Inbred BALB C,
pubmed-meshheading:2536919-Models, Molecular,
pubmed-meshheading:2536919-Molecular Sequence Data,
pubmed-meshheading:2536919-Mutation,
pubmed-meshheading:2536919-Oncogene Proteins, Viral,
pubmed-meshheading:2536919-Oncogenes,
pubmed-meshheading:2536919-Peptide Fragments,
pubmed-meshheading:2536919-Phosphoproteins,
pubmed-meshheading:2536919-Precipitin Tests,
pubmed-meshheading:2536919-Protein Conformation,
pubmed-meshheading:2536919-Recombinant Fusion Proteins,
pubmed-meshheading:2536919-Simian virus 40,
pubmed-meshheading:2536919-Viral Matrix Proteins
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pubmed:year |
1989
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pubmed:articleTitle |
The multiple membrane-spanning segments of the BNLF-1 oncogene from Epstein-Barr virus are required for transformation.
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pubmed:affiliation |
McArdle Laboratory for Cancer Research, University of Wisconsin-Madison 53706.
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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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