Tumor suppressor p53 gene forms multiple isoforms: Evidence for single lucus origin and cytoplasmic complex formation with heat shock proteins
| Autor: | Merrick Ba, Selkirk Jk, Rachel M. Patterson, He C |
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| Rok vydání: | 1996 |
| Předmět: |
Gene isoform
Cytoplasm Macromolecular Substances Clinical Biochemistry Breast Neoplasms Biology Biochemistry Analytical Chemistry Retinoblastoma-like protein 1 HSPA4 Mice Heat shock protein Tumor Cells Cultured Animals Humans Point Mutation Electrophoresis Gel Two-Dimensional HSP90 Heat-Shock Proteins Phosphorylation Mice Knockout HSPA12A Carcinoma Ductal Breast Cell Cycle Biological Transport Genes p53 Phosphoproteins Hsp90 Molecular biology Neoplasm Proteins Hsp70 Pleural Effusion biology.protein Female Tumor Suppressor Protein p53 Protein Processing Post-Translational |
| Zdroj: | Electrophoresis. 17:1764-1771 |
| ISSN: | 1522-2683 0173-0835 |
| DOI: | 10.1002/elps.1150171114 |
| Popis: | The tumor suppressor protein p53 is a major cell cycle control factor, and mutations in p53 are the most common genetic lesion found in human tumors, resulting in loss of function and contributing to malignant transformation. This report reviews several studies which show that p53 protein appears as at least eleven isoforms having the same amino acid backbone but varying in charge by level of phosphorylation. All isoforms are derived from a single locus, which indicates that p53 activity is modulated by post-translational modification. In addition, mutant p53 forms hetero-oligomers with two families of proteins: HSP70 and a 90 kDa group similar to HSP90. Cytoplasmic complexes are most likely formed to protect p53 from proteolysis and are probably involved in translocation of activated p53 from the cytoplasm to the nucleus for transactivation of other cell cycle control genes. |
| Databáze: | OpenAIRE |
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