Relationship of phosphorylation to the oligomerization of SV40 T antigen and its association with p53.
The potential significance of the phosphorylation of SV40 large T antigen for oligomers and complexes with the cellular protein p53 was investigated. We observed that T antigen oligomers remain stable after enzymatic dephosphorylation by alkaline phosphatase up to 80%. Separate analysis of free and p53-bound T antigen revealed a considerably lower phosphorylation of the p53-bound subclass. Therefore, a simple correlation between the overall phosphorylation of T antigen and the formation of oligomers and T-p53 complexes is highly unlikely.
Stürzbecher
H W
HW
Mörike
M
M
Montenarh
M
M
Henning
R
R
D000952:Antigens, Polyomavirus Transforming; D000957:Antigens, Viral, Tumor / Q000378:metabolism*; D002460:Cell Line; D002472:Cell Transformation, Viral; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D009363:Neoplasm Proteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011108:Polymers / Q000378:metabolism; D013539:Simian virus 40; D016159:Tumor Suppressor Protein p53; D014764:Viral Proteins / Q000378:metabolism*
D000952:Antigens, Polyomavirus Transforming; D000957:Antigens, Viral, Tumor; D009363:Neoplasm Proteins; D010750:Phosphoproteins; D011108:Polymers; D016159:Tumor Suppressor Protein p53; D014764:Viral Proteins