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Sci. STKE, 4 September 2007
Vol. 2007, Issue 402, p. tw321
[DOI: 10.1126/stke.4022007tw321]

EDITORS' CHOICE

Structural Biology Intricacies of Cell Contacts

Valda J. Vinson

Science, AAAS, Washington, DC 20005, USA

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]

Citation: V. J. Vinson, Intricacies of Cell Contacts. Sci. STKE 2007, tw321 (2007).

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