ArticleMolecular and cellular biology1993
Evidence that the middle T antigen of polyomavirus interacts with the membrane skeleton.
Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- 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
- Polyomavirus middle T antigen induces the transcription of osteopontin, a gene important for the migration of transformed cells.Journal of virology · 2008Article
- Natural biology of polyomavirus middle T antigen.Microbiology and molecular biology reviews : MMBR · 2001Review
- Article
- Signaling from polyomavirus middle T and small T defines different roles for protein phosphatase 2A.Molecular and cellular biology · 1998Article
- Bcl-2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types.The EMBO journal · 1996Article
- Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane.The EMBO journal · 1995Article
- Targeting of passenger protein domains to multiple intracellular membranes.The Biochemical journal · 1994Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transforming protein of polyomavirus, middle T antigen, is associated with cellular membranes. We have examined the subcellular location of the middle T antigen in two different cell types by fractionation and detergent phase partitioning. Middle T antigen expressed in human cells by a recombinant adenovirus was detected primarily in the membrane skeleton. Sucrose gradient fractionation revealed that the middle T antigen was associated with complexes with molecular weights of 500,000 to 1,000,000. Several markers for cytoskeleton cofractionate with these complexes, including actin, tubulin, and vimentin. Electron micrographs of membrane skeleton prepared from cells expressing middle T antigen demonstrated that this material contained primarily fibrous structures and was clearly devoid of bilayer membranes. These structures were distinct from the filamentous structures observed in fractions enriched for cytoskeleton. Consistent with a role for membrane skeleton localization in transformation, middle T antigen was detected exclusively in fractions enriched for membrane skeleton in middle T antigen-transformed Rat-2 cells. Our results may resolve the apparent difference between middle T antigen localization as determined by immunomicroscopy and that determined by subcellular fractionation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.