The block of adipocyte differentiation by a C-terminally truncated, but not by full-length, simian virus 40 large tumor antigen is dependent on an intact retinoblastoma susceptibility protein family binding domain
| ISSN: | 1098-5514 0022-538X |
|---|---|
| Přístupová URL adresa: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75dd9c9043ed22e72afd025816c1f1bb https://doi.org/10.1128/jvi.70.2.745-752.1996 |
| Rights: | OPEN |
| Přírůstkové číslo: | edsair.doi.dedup.....75dd9c9043ed22e72afd025816c1f1bb |
| Autor: | Sanjukta Chatterjee, V. Cherington, C. Higgins |
| Rok vydání: | 1996 |
| Předmět: |
Protein family
Antigens Polyomavirus Transforming Cellular differentiation Molecular Sequence Data Immunology Cell Count Simian virus 40 Retinoblastoma Protein Microbiology 3T3 cells Mice Virology Adipocytes Cell Adhesion medicine Animals Neoplastic transformation Binding Sites Base Sequence biology Retinoblastoma protein Cell Differentiation 3T3 Cells Molecular biology Peptide Fragments Tumor antigen medicine.anatomical_structure Cell culture Insect Science DNA Viral Mutation biology.protein Research Article Binding domain |
| Zdroj: | Journal of Virology. 70:745-752 |
| ISSN: | 1098-5514 0022-538X |
| Popis: | Simian virus 40 (SV40) can promote cell transformation and suppress differentiation. It does this partly by targeting tumor suppressors such as p53 and members of the retinoblastoma susceptibility protein (Rb) family. This work concentrates on mechanisms by which SV40 large tumor antigen (SVLT) suppresses adipocyte differentiation. We created cell lines derived from murine 3T3-L1 preadipocytes expressing different versions of SV40 early-region sequences. SVLT-expressing cells failed to exhibit adipocyte morphology, to induce glycerophosphate dehydrogenase activity, and to induce differentiation-dependent mRNA for adipocyte P2. SVLT alone was sufficient, in the absence of SV40 small tumor antigen, to inhibit differentiation. A truncated SVLT containing only the N-terminal 121 amino acids (SVLT1-121) blocked differentiation, thus mapping at least one differentiation blocking function to the N-terminal region. K1 (Glu-107-->Lys) point mutants of SVLT, which are unable to bind to the Rb protein family or induce neoplastic transformation, are defective for blocking differentiation in the case of SVLT1-121 but retain the ability to block differentiation in the case of full-length SVLT. This finding demonstrates that Rb family proteins are important in regulating adipocyte differentiation but that other functions of full-length SVLT can block adipocyte differentiation independently of RB family binding and transformation. |
| Databáze: | OpenAIRE |
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