Abstract |
A small fraction of polyoma virus middle-sized tumor ( T) antigen is phosphorylated in vivo, resulting in a small amount of phosphotyrosine and phosphothreonine and significantly larger amounts of phosphoserine. When infected cells are separated into nuclear, plasma membrane, and low-speed supernatant fractions, 80-95% of in vivo-phosphorylated middle-sized T antigen is localized to the plasma membrane fraction, while 25-50% of [35S] methionine-labeled middle-sized T antigen is found in the nuclear fraction and the same amount is found in the plasma membrane fraction. Immunoprecipitated T antigens contain a protein kinase activity that phosphorylates middle-sized T antigen at tyrosine residues. Eighty to 90% of this activity is located in the plasma membrane fraction. When immunoprecipitated T antigens are treated with alkaline phosphatase, middle-sized T antigen-phosphorylating activity decreases as 32PO4 is lost from in vivo 32P-labeled middle-sized T antigen. The possibility that in vivo-phosphorylated middle-sized T antigen located in the plasma membrane is an active tyrosine-specific kinase is discussed.
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Authors | K Segawa, Y Ito |
Journal | Proceedings of the National Academy of Sciences of the United States of America
(Proc Natl Acad Sci U S A)
Vol. 79
Issue 22
Pg. 6812-6
(Nov 1982)
ISSN: 0027-8424 [Print] United States |
PMID | 6294653
(Publication Type: Journal Article)
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Chemical References |
- Amino Acids
- Antigens, Viral
- Antigens, Viral, Tumor
- Protein Kinases
- Alkaline Phosphatase
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Topics |
- Alkaline Phosphatase
- Amino Acids
(analysis)
- Animals
- Antigens, Viral
(analysis, isolation & purification)
- Antigens, Viral, Tumor
- Cells, Cultured
- Mice
- Molecular Weight
- Phosphorylation
- Polyomavirus
(enzymology, immunology)
- Protein Kinases
(metabolism)
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