ArticleJournal of virology1995
Amino-terminal regions of polyomavirus middle T antigen are required for interactions with protein phosphatase 2A.
Article in Journal of virology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- The polyomavirus middle T-antigen oncogene activates the Hippo pathway tumor suppressor Lats in a Src-dependent manner.Oncogene · 2015Article
- Lessons in signaling and tumorigenesis from polyomavirus middle T antigen.Microbiology and molecular biology reviews : MMBR · 2009Review
- Lessons from polyoma middle T antigen on signaling and transformation: A DNA tumor virus contribution to the war on cancer.Virology · 2009Review
- Leucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in mammalian cells.The Journal of biological chemistry · 2007Article
- Genetic analysis of the polyomavirus DnaJ domain.Journal of virology · 2005Article
- Review
- Review
- Role of middle T-small T in the lytic cycle of polyomavirus: control of the early-to-late transcriptional switch and viral DNA replication.Journal of virology · 2001Article
- Natural biology of polyomavirus middle T antigen.Microbiology and molecular biology reviews : MMBR · 2001Review
- Effect on polyomavirus T-antigen function of mutations in a conserved leucine-rich segment of the DnaJ domain.Journal of virology · 2001Article
- Adenovirus E4 open reading frame 4-induced apoptosis involves dysregulation of Src family kinases.The Journal of cell biology · 2000Article
- Role of janus kinase-2 in insulin-mediated phosphorylation and inactivation of protein phosphatase-2A and its impact on upstream insulin signalling components.The Biochemical journal · 1999Article
- Catalytically inactive protein phosphatase 2A can bind to polyomavirus middle tumor antigen and support complex formation with pp60(c-src).Journal of virology · 1999Article
- Association between src-kinases and the polyoma virus oncogene middle T-antigen requires PP2A and a specific sequence motif.Oncogene · 1999Article
- Formation of transformed endothelial cells in the absence of VEGFR-2/Flk-1 by Polyoma middle T oncogene.Oncogene · 1999Article
- A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A.The Journal of biological chemistry · 1999Article
- Binding specificity of protein phosphatase 2A core enzyme for regulatory B subunits and T antigens.Journal of virology · 1999Article
- Signaling from polyomavirus middle T and small T defines different roles for protein phosphatase 2A.Molecular and cellular biology · 1998Article
- Tiny T antigen: an autonomous polyomavirus T antigen amino-terminal domain.Journal of virology · 1997Article
- pp60c-src binding to polyomavirus middle T-antigen (MT) requires residues 185 to 210 of the MT sequence.Journal of virology · 1997Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Polyomavirus middle T antigen (MT) is the major transforming protein of the virus. It functions through interactions with a number of cellular proteins involved in cell proliferation. MT forms complexes with protein phosphatase 2A (PP2A), pp60c-src, phosphatidylinositol 3-kinase, and Shc. We introduced both deletion and point mutations into three regions of MT and examined their ability to associate with PP2A and pp60c-src. The first 25 amino acid residues of MT are required for association with PP2A and pp60c-src. Amino acids 105 to 111, comprising the sequence Cys-Arg-Met-Pro-Leu-Thr-Cys, is also required for complex formation between MT and PP2A. However, the sequence Asp-Lys-Gly-Gly (amino acids 44 to 47), also found in the B subunit of PP2A, is dispensable for complex formation between MT and PP2A. We find a strict correlation between the ability of MT to associate with PP2A and the ability of MT to associate with pp60c-src. One mutant, L5E, associates with a phosphatase other than PP2A, pp60c-src, and phosphatidylinositol 3-kinase in a manner similar to that of wild-type MT yet is reduced in its transforming ability on NIH 3T3 cells.
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