Editors' ChoiceStructural Biology

Intricacies of Cell Contacts

Science's STKE  04 Sep 2007:
Vol. 2007, Issue 402, pp. tw321
DOI: 10.1126/stke.4022007tw321

Cell-cell contacts in multicellular organisms are intricately regulated, and their stability is partly controlled by protein kinases and phosphatases that tune the level of tyrosine phosphorylation. Type II B receptor protein tyrosine phosphatases (RPTPs) have both adhesive and catalytic properties. Aricescu et al. determined the crystal structure of the full-length extracellular region of an RPTP, which forms a homophilic trans dimer that is rigid and has dimensions that match the intercellular distance at cadherin-mediated junctions. The trans interaction may act as a spacer clamp that localizes phosphatase activity near its target substrates.

A. R. Aricescu, C. Siebold, K. Choudhuri, V. T. Chang, W. Lu, S. J. Davis, P. A. van der Merwe, E. Y. Jones, Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism. Science 317, 1217-1220 (2007). [Abstract] [Full Text]