A Novel Group IIA Phospholipase A2Interacts with v-Src Oncoprotein from RSV-transformed Hamster Cells
| Autor: | Olga A. Mizenina, Yuriy G. Yanushevich, Jacques Camonis, Jean de Gunzburg, Anna Rodina, Michail A. Krasilnikov, Armand Tavitian, Elena Musatkina, A. G. Tatosyan |
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| Rok vydání: | 2001 |
| Předmět: |
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Complementary Recombinant Fusion Proteins Blotting Western Molecular Sequence Data Hamster SH2 domain Biochemistry Avian sarcoma virus Phospholipases A Cell Line Oncogene Protein pp60(v-src) Cricetinae Two-Hybrid System Techniques Animals Amino Acid Sequence Amino Acids Phosphorylation Tyrosine Molecular Biology Cell Line Transformed Gene Library Glutathione Transferase Rous sarcoma virus Phospholipase A Base Sequence Mesocricetus Sequence Homology Amino Acid biology Cell Biology Fibroblasts Blotting Northern biology.organism_classification Precipitin Tests Molecular biology Protein Structure Tertiary Phospholipases A2 Avian Sarcoma Viruses v-Src Protein Binding Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Journal of Biological Chemistry. 276:34006-34012 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m011320200 |
| Popis: | We have isolated a novel isoform of phospholipase A(2). This enzyme was designated srPLA(2) because it was discovered while analyzing the proteins interacting with different forms of the v-Src oncoproteins isolated from Rous sarcoma virus-transformed hamster cells. It contains all the functional regions of the PLA(2) group IIA proteins but differs at its C-terminal end where there is an additional stretch of 8 amino acids. The SrPLA(2) isoform was detected as a 17-kDa precursor in cells and as a mature 14-kDa form secreted in culture medium. A direct interaction of the 17-kDa precursor with the Src protein was observed in lysates of transformed cells. Both the 17- and 14-kDa forms were found to be phosphorylated on tyrosine. To our knowledge, this is the first report of a PLA(2) group II protein that is tyrosine phosphorylated. We surmise that srPLA(2) interacts with the Src protein at the cell membrane during the process of its maturation. |
| Databáze: | OpenAIRE |
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