Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding.
Research output: Contribution to journal › Journal article › Research › peer-review
Receptor tyrosine phosphatases (R-PTPases) feature PTPase domains in the context of a receptor-like transmembrane topology. The R-PTPase R-PTP-kappa displays an extracellular domain composed of fibronectin type III motifs, a single immunoglobulin domain, as well as a recently defined MAM domain (Y.-P. Jiang, H. Wang, P. D'Eustachio, J.M. Musacchio, J. Schlessinger, and J. Sap, Mol. Cell. Biol. 13:2942-2951, 1993). We report here that R-PTP-kappa can mediate homophilic intercellular interaction. Inducible expression of the R-PTP-kappa protein in heterologous cells results in formation of stable cellular aggregates strictly consisting of R-PTP-kappa-expressing cells. Moreover, the purified extracellular domain of R-PTP-kappa functions as a substrate for adhesion by cells expressing R-PTP-kappa and induces aggregation of coated synthetic beads. R-PTP-kappa-mediated intercellular adhesion does not require PTPase activity or posttranslational proteolytic cleavage of the R-PTP-kappa protein and is calcium independent. The results suggest that R-PTPases may provide a link between cell-cell contact and cellular signaling events involving tyrosine phosphorylation.
Original language | English |
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Journal | Molecular and Cellular Biology |
Volume | 14 |
Issue number | 1 |
Pages (from-to) | 1-9 |
Number of pages | 8 |
ISSN | 0270-7306 |
Publication status | Published - 1994 |
Bibliographical note
Keywords: Animals; Cell Adhesion; Cell Aggregation; Cell Communication; Cell Line; DNA, Complementary; Drosophila melanogaster; Extracellular Space; Gene Expression; Humans; Mice; Protein Conformation; Protein Tyrosine Phosphatases; Receptor-Like Protein Tyrosine Phosphatases, Class 2; Recombinant Proteins; Transfection
ID: 5069965