Abstract
In latently infected growth-transformed human lymphocytes, Epstein-Barr virus (EBV) encodes two integral plasma membrane proteins: LMP1, which constitutively induces B-lymphocyte activation and intercellular adhesion, and LMP2A, which associates with LMP1 and is a tyrosine kinase substrate. We now demonstrate that LMP2A associates with src family protein tyrosine kinases, particularly lyn kinase, in nonionic detergent extracts of transfected B lymphoma cells or in extracts of EBV-transformed B lymphocytes. The LMP2A and tyrosine kinase association is stable in nonionic detergents and includes a 70-kDa cell protein which is also an in vitro or in vivo kinase substrate. This LMP2A association with B-lymphocyte src family tyrosine kinases is likely to be an important pathway in EBV's effects on cell growth.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Antigens, Viral / genetics
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Antigens, Viral / isolation & purification
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Antigens, Viral / metabolism*
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B-Lymphocytes
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Cell Line
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Cell Transformation, Viral*
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Genes, src*
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Herpesvirus 4, Human / metabolism*
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Lymphoma, B-Cell
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Membrane Proteins / genetics
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Membrane Proteins / isolation & purification
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Membrane Proteins / metabolism*
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Oncogene Protein pp60(v-src) / isolation & purification
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Oncogene Protein pp60(v-src) / metabolism*
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Protein Binding
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Protein-Tyrosine Kinases / isolation & purification
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Protein-Tyrosine Kinases / metabolism*
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Transfection
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Viral Matrix Proteins*
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Viral Proteins / genetics
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Viral Proteins / isolation & purification
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Viral Proteins / metabolism*
Substances
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Antigens, Viral
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EBV-associated membrane antigen, Epstein-Barr virus
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Membrane Proteins
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Viral Matrix Proteins
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Viral Proteins
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Protein-Tyrosine Kinases
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Oncogene Protein pp60(v-src)