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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Alternative splicing gives rise to a nuclear protein tyrosine phosphatase in Drosophila.

A novel Drosophila protein tyrosine phosphatase gene (dPTP61F) undergoes alternative splicing to encode two non-receptor-like proteins of 61,000 daltons. This splice selection occurs at the 3' end of the message, altering the carboxyl termini of the encoded proteins. These carboxyl-terminal sequences govern the targeting of each protein tyrosine phosphatase either to a cytoplasmic membrane or to the nucleus. The catalytic activity of the two protein products is indistinguishable, suggesting that substrate specificity is modulated by the protein's subcellular location.[1]

References

  1. Alternative splicing gives rise to a nuclear protein tyrosine phosphatase in Drosophila. McLaughlin, S., Dixon, J.E. J. Biol. Chem. (1993) [Pubmed]
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