The human cot proto-oncogene encodes two protein serine/threonine kinases with different transforming activities by alternative initiation of translation
| Autor: | Masahiro Aoki, Shuji Sumida, Tetsu Akiyama, Kumao Toyoshima, Fumihiko Hamada, Toshiro Sugimoto |
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| Rok vydání: | 1993 |
| Předmět: |
DNA
Complementary Molecular Sequence Data Gene Expression Protein Serine-Threonine Kinases Sulfur Radioisotopes Transfection Biochemistry Polymerase Chain Reaction Proto-Oncogene Mas AKT3 Cell Line DDB1 Open Reading Frames Methionine Cricetinae Proto-Oncogene Proteins SNAP23 HSPA2 Proto-Oncogenes Tumor Cells Cultured Animals Humans Amino Acid Sequence Peptide Chain Initiation Translational Molecular Biology DNA Primers Serine/threonine-specific protein kinase Gene Rearrangement biology Base Sequence GRB10 Cell Biology MAP Kinase Kinase Kinases Phosphoproteins EIF4EBP1 Cell Transformation Neoplastic GATAD2B biology.protein Mutagenesis Site-Directed Autoradiography Baculoviridae |
| Zdroj: | The Journal of biological chemistry. 268(30) |
| ISSN: | 0021-9258 |
| Popis: | The cot gene is an oncogene encoding serine/threonine kinases isolated by DNA transfection assay. In this study, we isolated cDNA for the human cot protooncogene (proto-cot gene) and examined the structure and function of its gene products. The proto-cot gene has an open reading frame encoding 467 amino acids of which the first 397 amino acids are identical to those in the corresponding part of the cot gene. The protein products of the proto-cot gene were identified as 58- and 52-kDa proteins with intrinsic protein serine/threonine kinase activity. These two protein species were suggested to be generated by alternative initiation from two AUGs. The 58- and 52-kDa proteins are both localized predominantly in the cytosol, but the 58-kDa protein has a shorter half-life than the 52-kDa protein, suggesting the importance of the amino-terminal domain in regulating the stability of the proto-Cot protein. More interestingly, the 58-kDa protein showed stronger transforming activity than the 52-kDa protein, although this activity was much weaker than that of the Cot oncoprotein. Thus, the amino-terminal domain of the Cot protein may be necessary for cellular transformation, whereas the carboxyl-terminal domain may negatively regulate the transforming activity. |
| Databáze: | OpenAIRE |
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