A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila

• Published in: Proceedings of the National Academy of Sciences - PNAS 1989-11, Vol.86 (22), p.8698-8702
• Main Authors: Streuli, M. (Harvard Medical School, Boston, MA), Krueger, N.X, Tsai, A.Y.M, Saito, H
• Format: Article
• Language: English
• Subjects: 550201 - Biochemistry- Tracer Techniques; AMINO ACID SEQUENCE; AMINO ACIDS; ANGIOTENSIN; ANIMALS; Antibodies; ANTIGENS; ARTHROPODS; BACTERIA; BASIC BIOLOGICAL SCIENCES; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; Biological and medical sciences; CARBOXYLIC ACIDS; CARDIOVASCULAR AGENTS; CELL CONSTITUENTS; Cell growth; CELL PROLIFERATION; CHEMICAL REACTIONS; Cloning, Molecular; Complementary DNA; CYSTEINE; DAYS LIVING RADIOISOTOPES; DIPTERA; DLAR gene; DNA; DNA - genetics; DNA - isolation & purification; DPTP gene; DROSOPHILA; Drosophila melanogaster; Drosophila melanogaster - enzymology; Drosophila melanogaster - genetics; Drosophilidae; DRUGS; ENZYME ACTIVITY; ENZYMES; ESCHERICHIA COLI; Escherichia coli - enzymology; Escherichia coli - genetics; ESTERASAS; ESTERASE; ESTERASES; FLIES; FRUIT FLIES; Fundamental and applied biological sciences. Psychology; Gene Expression; Gene expression regulation; GENERO HUMANO; GENES; Genes. Genome; GENRE HUMAIN; GLOBULINS; Humans; HYDROXY ACIDS; INSECTS; INVERTEBRATES; ISOTOPES; Kinetics; LIGHT NUCLEI; MAMMALS; MAN; MANKIND; MEMBRANE PROTEINS; MICROORGANISMS; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; MOLECULAR STRUCTURE; Molecules; Multigene Family; MUTAGENESIS; NUCLEI; NUCLEIC ACIDS; nucleotide sequence; ODD-ODD NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC SULFUR COMPOUNDS; Phosphatases; Phosphoprotein Phosphatases - genetics; Phosphoprotein Phosphatases - metabolism; PHOSPHORUS 32; PHOSPHORUS ISOTOPES; PHOSPHORUS-GROUP TRANSFERASES; PHOSPHORYLATION; PHOSPHOTRANSFERASES; PLASMIDS; PRIMATES; Protein isoforms; Protein Tyrosine Phosphatases; protein-tyrosine phosphatase; PROTEINAS; PROTEINE; PROTEINS; RADIOISOTOPES; RECEPTORS; RECOMBINANT DNA; Restriction Mapping; Sequence Homology, Nucleic Acid; THIOLS; TIROSINA; TRANSFERASES; TYROSINE; VASOCONSTRICTORS; VERTEBRATES
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.86.22.8698

To understand the regulation of cell proliferation by tyrosine phosphorylation, characterization of protein tyrosine phosphatases (PTPase; protein-tyrosine-phosphate phosphohydrolase, EC 3.1.3.48) is essential. The human genes LCA (leukocyte common antigen) and LAR encode putative receptor-linked PTPases. By using consensus sequence probes, two additional receptor-linked PTPase genes, DLAR and DPTP, were isolated from Drosophila melanogaster. The extracellular segments of both DLAR and DPTP are composed of multiple immunoglobulin-like domains and fibronectin type III-like domains. The cytoplasmic region of DLAR and DPTP, as well as human LCA and LAR, are composed of two tandemly repeated PTPase domains. PTPase activities of immunoprecipitated LCA and LAR were demonstrated by measuring the release of phosphate from a 32P-labeled [Tyr(P)]peptide. Furthermore, the cytoplasmic domains of LCA, LAR, DLAR, and DPTP, expressed in Escherichia coli, have PTPase activity. Site-directed mutagenesis showed that a conserved cysteine residue is essential for PTPase activity.