Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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

DOI

10.1126/science.1144646

Type

Journal article

Journal

Science

Publication Date

31/08/2007

Volume

317

Pages

1217 - 1220

Keywords

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