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.
McLaughlin
S
S
University of Michigan Medical School, Department of Biological Chemistry, Ann Arbor.
Dixon
J E
JE
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D002467:Cell Nucleus / Q000201:enzymology; D004247:DNA; D004330:Drosophila; D005455:Fluorescent Antibody Technique; D006801:Humans; D008969:Molecular Sequence Data; D010766:Phosphorylation; D017027:Protein Tyrosine Phosphatases / Q000235:genetics* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D004247:DNA; D017027:Protein Tyrosine Phosphatases