Receptor tyrosine phosphatase R-PTP-K mediates homophilic binding

Jan Sap, Ying Ping Jiang, David Friedlander, Martin Grumet, Joseph Schlessinger

Research output: Contribution to journalArticlepeer-review

188 Scopus citations

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 languageAmerican English
Pages (from-to)1-9
Number of pages9
JournalMolecular and cellular biology
Volume14
Issue number1
StatePublished - 1994
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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