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J. Biol. Chem., Vol. 276, Issue 36, 34006-34012, September 7, 2001

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A Novel Group IIA Phospholipase A₂ Interacts with v-Src Oncoprotein from RSV-transformed Hamster Cells^*

Olga Mizenina^§, Elena Musatkina, Yuriy Yanushevich, Anna Rodina, Michail Krasilnikov, Jean de Gunzburg^¶, Jacques H. Camonis^¶, Armand Tavitian^¶, and Alexander Tatosyan

From the  Institute of Carcinogenesis, Cancer Research Center, Kashirskoye shosse, 24, 115 478, Moscow, Russia and ^¶ INSERM, U548, Institut Curie, 26 rue d'Ulm, 75248, Paris Cedex 05, France

We have isolated a novel isoform of phospholipase A₂. This enzyme was designated srPLA₂ 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 PLA₂ group IIA proteins but differs at its C-terminal end where there is an additional stretch of 8 amino acids. The SrPLA₂ 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 PLA₂ group II protein that is tyrosine phosphorylated. We surmise that srPLA₂ interacts with the Src protein at the cell membrane during the process of its maturation.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AJ251361.

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