Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism

Science

Volumn 317, Issue 5842, 2007, Pages 1217-1220

  Aricescu, A Radu ^a   Siebold, Christian ^a   Choudhuri, Kaushik ^b   Chang, Veronica T ^c   Lu, Weixian ^a   Davis, Simon J ^c   Van Der Merwe, P Anton ^b   Jones, E Yvonne ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CADHERIN; CATENIN; PROTEIN TYROSINE PHOSPHATASE; CELL ADHESION MOLECULE; FIBRONECTIN; IMMUNOGLOBULIN; PROTEIN TYROSINE PHOSPHATASE, RECEPTOR TYPE M; UNCLASSIFIED DRUG;

AMINO ACID; CRYSTAL STRUCTURE; ENZYME ACTIVITY; PROTEIN;

ARTICLE; CELL ADHESION; CELL AGGREGATION; CELL INTERACTION; CELL SURFACE; CRYSTAL STRUCTURE; ENZYME STRUCTURE; GLYCOSYLATION; HUMAN; HYDROGEN BOND; HYDROPHILICITY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; AMINO ACID SEQUENCE; CELL JUNCTION; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ENZYMOLOGY; GENETICS; HYDROPHOBICITY; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PH; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; ULTRASTRUCTURE;

ADHERENS JUNCTIONS; AMINO ACID SEQUENCE; CELL ADHESION; CELL ADHESION MOLECULES; CELL MEMBRANE; CONSERVED SEQUENCE; DIMERIZATION; FIBRONECTINS; HUMANS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; IMMUNOGLOBULINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; PROTEIN-TYROSINE-PHOSPHATASE;

EID: 34548539380     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1144646     Document Type: Article

References (37)

1. M. Perez-Moreno, C. Jamora, E. Fuchs, Cell 112, 535 (2003).
2. B. M. Gumbiner, Nat. Rev. Mol. Cell Biol. 6, 622 (2005).
3. J. L. Sallee, E. S. Wittchen, K. Burridge, J. Biol. Chem. 281, 16189 (2006).
4. R. L. Del Vecchio, N. K. Tonks, J. Biol. Chem. 280, 1603 (2005).
5. M. F. Gebbink et al., J. Cell Biol. 131, 251 (1995).
6. N. K. Tonks, Nat. Rev. Mol. Cell Biol. 7, 833 (2006).
7. J. Besco, M. C. Popesco, R. V. Davuluri, A. Frostholm, A. Rotter, BMC Genomics 5, 14 (2004).
8. A. R. Aricescu et al., EMBO J. 25, 701 (2006).
9. A. R. Aricescu, W. Lu, E. Y. Jones, Acta Crystallogr. D 62, 1243 (2006).
10. V. T. Chang et al., Structure 15, 267 (2007).
11. Materials and methods are available as supporting material on Science Online.
12. V. Soroka et al., Structure 11, 1291 (2003).
13. M. Campan et al., Biochemistry 35, 3797 (1996).
14. L. Anders et al., Mol. Cell. Biol. 26, 3917 (2006).
15. V. B. Cismasiu, S. A. Denes, H. Reilander, H. Michel, S. E. Szedlacsek, J. Biol. Chem. 279, 26922 (2004).
16. S. M. Brady-Kalnay, A. J. Flint, N. K. Tonks, J. Cell Biol. 122, 961 (1993).
17. J. Cheng et al., J. Biol. Chem. 272, 7264 (1997).
18. M. F. Gebbink et al., J. Biol. Chem. 268, 16101 (1993).
19. G. C. M. Zondag et al., J. Biol. Chem. 270, 14247 (1995).
20. J. Sap, Y. P. Jiang, D. Friedlander, M. Grumet, J. Schlessinger, Mol. Cell. Biol. 14, 1 (1994).
21. M. Fuchs, H. Wang, T. Ciossek, Z. Chen, A. Ullrich, Mech. Dev. 70, 91 (1998).
22. Z. Wang et al., Science 304, 1164 (2004).
23. J. A. Besco, R. Hooft van Huijsduijnen, A. Frostholm, A. Rotter, Brain Res. 1116, 50 (2006).
24. M. Fuchs, T. Muller, M. M. Lerch, A. Ullrich, J. Biol. Chem. 271, 16712 (1996).
25. G. C. M. Zondag, A. B. Reynolds, W. H. Moolenaar, J. Biol. Chem. 275, 11264 (2000).
26. S. M. Brady-Kalnay et al., J. Cell Biol. 141, 287 (1998).
27. X. F. Sui et al., Am. J. Pathol. 166, 1247 (2005).
28. K. Miyaguchi, J. Struct. Biol. 132, 169 (2000).
29. T. J. Boggon et al., Science 296, 1308 (2002).
30. L. A. Staehelin, Int. Rev. Cytol. 39, 191 (1974).
31. W. He, P. Cowin, D. L. Stokes, Science 302, 109 (2003).
32. I. A. Yudushkin et al., Science 315, 115 (2007).
33. S. J. Davis, P. A. van der Merwe, Nat. Immunol. 7, 803 (2006).
34. K. Choudhuri, D. Wiseman, M. H. Brown, K. Gould, P. A. van der Merwe, Nature 436, 578 (2005).
35. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
36. T. Maretzky et al., Proc. Natl. Acad. Sci. U.S.A. 102, 9182 (2005).
37. - cell line; M. Shaw for assistance with EM imaging; and J. Brown, M. Crispin, W.-C. Hon, and D. Stuart for discussions. The work was funded by Cancer Research UK (CR-UK). E.Y.J. is a CR-UK Principal Research Fellow.