Abstract
Receptor tyrosine phosphatases (R-PTPases) feature PTPase domains in the context of a receptor-like transmembrane topology. The R-PTPase R-PTP-κ displays an extracellular domain composed of fibronectin type in 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-κ can mediate homophilic intercellular interaction. Inducible expression of the R-PTP-κ protein in heterologous cells results in formation of stable cellular aggregates strictly consisting of R-PTP-κ-expressing cells. Moreover, the purified extracellular domain of R-PTP-κ functions as a substrate for adhesion by cells expressing R-PTP-κ and induces aggregation of coated synthetic beads. R-PTP-κ-mediated intercellular adhesion does not require PTPase activity or posttranslational proteolytic cleavage of the R-PTP-κ 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 | American English |
---|---|
Pages (from-to) | 1-9 |
Number of pages | 9 |
Journal | Molecular and cellular biology |
Volume | 14 |
Issue number | 1 |
State | Published - 1994 |
Externally published | Yes |
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology