Tandem PDZ repeats in glutamate receptor-interacting proteins have a novel mode of PDZ domain-mediated target binding

Nature Structural Biology

Volumn 10, Issue 11, 2003, Pages 972-978

  Feng, Wei ^a   Shi, Yawei ^a   Li, Ming ^a   Zhang, Mingjie ^a  

^a HONG KONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Hong Kong)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE RECEPTOR; GLUTAMATE RECEPTOR 2; GLUTAMATE RECEPTOR 3; GLUTAMATE RECEPTOR INTERACTING PROTEIN; PROTEIN PDZ4; PROTEIN PDZ5; RECEPTOR PROTEIN; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; COVALENT BOND; ISOLATION PROCEDURE; MEMBRANE TRANSPORT; MOLECULAR MODEL; MOLECULAR RECOGNITION; MOLECULAR STABILITY; NONHUMAN; ORIENTATION; PDZ DOMAIN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN STABILITY; RAT; RECEPTOR BINDING; SYNAPTIC MEMBRANE;

AMINO ACID SEQUENCE; ANIMALS; CARRIER PROTEINS; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RATS;

ANIMALIA;

EID: 0242407128     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb992     Document Type: Article

References (46)

1. Zhang, M. & Wang, W. Organization of signaling complexes by PDZ-domain scaffold proteins. Acc. Chem. Res. 36, 530-538 (2003).
2. Craven, S.E. & Bredt, D.S. PDZ proteins organize synaptic signaling pathways. Cell 93, 495-498 (1998).
3. Garner, C.C., Nash, J. & Huganir, R.L. PDZ domains in synapse assembly and signalling. Trends Cell Biol. 10, 274-280 (2000).
4. Sheng, M. & Sala, C. PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24, 1-29 (2001).
5. Doyle, D.A. et al. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 85, 1067-1076 (1996).
6. Harris, B.Z. & Lim, W.A. Mechanism and role of PDZ domains in signaling complex assembly. J. Cell. Sci. 114, 3219-3231 (2001).
7. Tochio, H., Zhang, Q., Mandal, P., Li, M. & Zhang, M. Solution structure of the extended neuronal nitric oxide synthase PDZ domain complexed with an associated peptide. Nat. Struct. Biol. 6, 417-421 (1999).
8. Hillier, B.J., Christopherson, K.S., Prehoda, K.E., Bredt, D.S. & Lim, W.A. Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex. Science 284, 812-815 (1999).
9. Long, J.F. et al. Supramodular structure and synergistic target binding of the N-terminal tandem PBZ domains of PSD-95. J. Mol. Biol. 327, 203-214 (2003).
10. Zimmermann, P. et al. Characterization of syntenin, a syndecan-binding PDZ protein, as a component of cell adhesion sites and microfilaments. Mol. Biol. Cell 12, 339-350 (2001).
11. Okamoto, M. & Sudhof, T.C. Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. J. Biol. Chem. 272, 31459-31464 (1997).
12. Lau, K.F., McLoughlin, D.M., Standen, C. & Miller, C.C. X11 α and X11 β interact with presenilin-1 via their PDZ domains. Mol. Cell. Neurosci. 16, 557-565 (2000).
13. Grootjans, J.J., Reekmans, G., Ceulemans, H. & David, G. Syntenin-syndecan binding requires syndecan-synteny and the co-operation of both PDZ domains of syntenin. J. Biol. Chem. 275, 19933-19941 (2000).
14. Raghuram, V., Mak, D.O. & Foskett, J.K. Regulation of cystic fibrosis transmembrane conductance regulator single-channel gating by bivalent PDZ-domain-mediated interaction. Proc. Natl. Acad. Sci. USA 98, 1300-1305. (2001).
15. Geijsen, N. et al. Cytokine-specific transcriptional regulation through an IL-5Rα interacting protein. Science 293, 1136-1138 (2001).
16. Jannatipour, M. et al. Schwannomin isoform-1 interacts with syntenin via PDZ domains. J. Biol. Chem. 276, 33093-33100 (2001).
17. Dong, H. et al. GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature 386, 279-284 (1997).
18. Srivastava, S. et al. Novel anchorage of GluR2/3 to the postsynaptic density by the AMPA receptor-binding protein ABP. Neuron 21, 581-591 (1998).
19. Wyszynski, M. et al. Association of AMPA receptors with a subset of glutamate receptor-interacting protein in vivo. J. Neurosci. 19, 6528-6537 (1999).
20. Ye, B. et al. GRASP-1: a neuronal RasGEF associated with the AMPA receptor/GRIP complex. Neuron 26, 603-617 (2000).
21. Dong, H. et al. Characterization of the glutamate receptor-interacting proteins GRIP1 and GRIP2. J. Neurosci. 19, 6930-6941 (1999).
22. Osten, P. et al. Mutagenesis reveals a role for ABP/GRIP binding to GluR2 in synaptic surface accumulation of the AMPA receptor. Neuron 27, 313-325 (2000).
23. Daw, M.I. et al. PDZ proteins interacting with C-terminal GluR2/3 are involved in a PKC-dependent regulation of AMPA receptors at hippocampal synapses. Neuron 28, 873-886 (2000).
24. Zhang, Q., Fan, J.-S. & Zhang, M. Interdomain chaperoning between PSD-95, Dlg, and Zo-1 (PDZ) domains of glutamate receptor-interacting proteins. J. Biol. Chem. 276, 43216-43220 (2001).
25. Songyang, Z. et al. Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science 275, 73-77 (1997).
26. Xia, J., Zhang, X., Staudinger, J. & Huganir, R.L. Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1. Neuron 22, 179-187 (1999).
27. Hirbec, H. et al. Rapid and differential regulation of AMPA and kainate receptors at hippocampal mossy fibre synapses by PICK1 and GRIP. Neuron 37, 625-638 (2003).
28. Tochio, H., Hung, F., Li, M., Bredt, D.S. & Zhang, M. Solution structure and backbone dynamics of the second PDZ domain of postsynaptic density-95. J. Mol. Biol. 295, 225-237 (2000).
29. Kang, B.S. et al. PDZ tandem of human syntenin. Crystal structure and functional properties. Structure 11, 459-468 (2003).
30. Hatada, M.H. et al. Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor. Nature 377, 32-38 (1995).
31. Hof, P., Pluskey, S., Dhe-Paganon, S., Eck, M.J. & Shoelson, S.E. Crystal structure of the tyrosine phosphatase SHP-2. Cell 92, 441-450 (1998).
32. Ottinger, E.A., Botfield, M.C. & Shoelson, S.E. Tandem SH2 domains confer high specificity in tyrosine kinase signaling. J. Biol. Chem. 273, 729-235 (1998).
33. Jacobson, R.H., Ladurner, A.G., King, D.S. & Tjian, R. Structure and function of a human TAFII250 double bromodomain module. Science 288, 1422-1425 (2000).
34. Gardner, K.H. & Kay, L.E. The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annu. Rev. Biophys. Biomol. Struct. 27, 357-406 (1998).
35. Pervushin, K., Riek, R., Wider, G. & Wuthrich, K. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. USA 94, 12366-12371 (1997).
36. Kay, L.E. Nuclear magnetic resonance methods for high molecular weight proteins: a study involving a complex of maltose binding protein and β-cyclodextrin. Methods Enzymol. 339, 174-203 (2001).
37. Bax, A. & Grzesiek, S. Methodological advances in protein NMR. Acc. Chem. Res. 26, 131-138 (1993).
38. Kay, L.E. & Gardner, K.H. Solution NMR spectroscopy beyond 25 kDa. Curr. Opin. Struct. Biol. 7, 722-731 (1997).
39. Wüthrich, K. NMR of Proteins and Nucleic Acids (Wiley, New York, 1986).
40. Cornilescu, G., Delaglio, F. & Bax, A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302 (1999).
41. Brunger, A.T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
42. Koradi, R., Billeter, M. & Wuthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55 (1996).
43. Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
44. Merritt, E. & Murphy, M. Raster3D version 2.0: a program for photorealistic molecular graphics. Acta Crystallogr. D 50, 869-873 (1994).
45. Nicholls, A. GRASP: graphical representation and analysis of surface properties (Columbia University, New York, 1992).
46. Laskowski, R.A., Rullman, J.A., MacArthur, M.W., Kaptein, R. & Thornton, J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486 (1996).