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Differential subcellular localization of in vivo-phosphorylated and nonphosphorylated middle-sized tumor antigen of polyoma virus and its relationship to middle-sized tumor antigen phosphorylating activity in vitro.

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.
AuthorsK Segawa, Y Ito
JournalProceedings 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
PMID6294653 (Publication Type: Journal Article)
Chemical References
  • Amino Acids
  • Antigens, Viral
  • Antigens, Viral, Tumor
  • Protein Kinases
  • Alkaline Phosphatase
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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