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Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control. Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes. Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions. Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length. These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.

Original publication




Journal article



Publication Date





1217 - 1220


Adherens Junctions, Amino Acid Sequence, Cell Adhesion, Cell Adhesion Molecules, Cell Membrane, Conserved Sequence, Dimerization, Fibronectins, Humans, Hydrogen Bonding, Hydrogen-Ion Concentration, Hydrophobic and Hydrophilic Interactions, Immunoglobulins, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Structure, Tertiary, Protein Tyrosine Phosphatases, Receptor-Like Protein Tyrosine Phosphatases, Class 2