Polyomavirus middle-T antigen lacking a membrane anchor sequence accumulates in the nucleus

被引:11
作者
Messerschmitt, A [1 ]
Disela, C [1 ]
Dilworth, S [1 ]
Marti, AG [1 ]
BallmerHofer, K [1 ]
机构
[1] FRIEDRICH MIESCHER INST,CH-4002 BASEL,SWITZERLAND
关键词
D O I
10.1099/0022-1317-77-1-17
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Three proteins expressed early in the replicative cycle of polyomavirus also play an essential role during virused-mediated tumorigenesis. One of the proteins, middle-T antigen, has been shown to bind cellular proteins involved in cell signalling such as c-Src, phosphatase 2A, phosphatidylinositol 3-kinase and SHC. Association of middle-T antigen with cellular membranes has been shown to be essential for middle-T-mediated cell transformation. A mutant virus encoding a truncated form of middle-T lacking a carboxy-terminal hydrophobic sequence mediating membrane association is not oncogenic. This mutant middle-T still binds phosphatase 2A through amino-terminal sequences common to small- and middle-T and is localized in the nucleus, although the protein does not contain a classical nuclear targeting sequence. Mutations introduced into the amino-terminal domain affecting the ability of truncated middle-T to bind phosphatase 2A prevented accumulation of the protein in the nucleus and led to localization in the cytoplasm. This suggests that nuclear localization of truncated middle-T may be a consequence of binding to phosphatase 2A.
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页码:17 / 26
页数:10
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