Interaction of ion channels and receptors with PDZ domain proteins

Current Opinion in Neurobiology

Volumn 7, Issue 3, 1997, Pages 368-373

  Kornau, Hans Christian ^a   Seeburg, Peter H ^a   Kennedy, Mary B ^b  

^a MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

^b CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; MEMBRANE RECEPTOR;

NERVE CELL; NEUROANATOMY; PRIORITY JOURNAL; PROTEIN INTERACTION; REVIEW; SIGNAL TRANSDUCTION;

EID: 0030744829     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-4388(97)80064-5     Document Type: Article

References (35)

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13. 50 values for PDZ domain 1 (PDZ1), PDZ2 and PDZ3 of 30 nM, 6 nM and 1 μM, respectively. of special interest.
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15. Itoh M, Nagafuchi A, Yonemura S, Kitani-Yasuda T, Tsukita S, Tsukita S. The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunelectron microscopy. J Cell Biol. 3:1993;491-502.
16. Kornau H-C, Schenker LT, Kennedy MB, Seeburg PH. Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science. 269:1995;1737-1740.
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18. + channels by interaction with a family of membrane-associated guanylate kinases. Nature. 378:1995;85-88.
19. Doyle DA, Lee A, Lewis J, Kim E, Sheng M, MacKinnon R. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell. 85:1996;1067-1076 These authors determined by X-ray structures of the third PDZ domain of PSD-95 in the presence and absence of its peptide ligand at 1.8 Å and 2.3 Å resolution, respectively. In addition to the overall structures, this study revealed how mainchain and sidechain interaction between the PDZ domain and the bound peptide lead to a selective recognition of the carboxy-terminal consensus sequence. of outstanding interest.
20. Cabral JH, Petosa C, Sutcliffe MJ, Raza S, Byron O, Poy F, Marfatia SM, Chishti AH, Liddington RC. Crystal structure of a PDZ domain. Nature. 382:1996;649-652 Here, the crystal structure of the third PDZ domain of Hdlg is presented at 2.8 Å resolution. A hydrophobic pocket and a buried arginine are detected on the surface of the domain and predicted to be the binding site for the carboxy-terminal peptide. of outstanding interest.
21. Dong H, O'Brien RJ, Fung ET, Lanahan AA, Worley PF, Huganir RL. Isolation of GRIP, a synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature. 386:1997;279-284 This report describes a novel synaptic protein called GRIP (glutamate receptor interacting protein). GRIP was found in a two-hybrid screen with the carboxyl terminus of GluR-B as a bait and contains seven PDZ domains. Two of the PDZ domains and additional sequences are involved in binding to the carboxyl-terminal sequence SVKI* in AMPA receptor subunits GluR-B and GluR-C. GRIP is predicted to serve as an adaptor protein between AMPA receptors and other components. of outstanding interest.
22. Brakeman PR, Lanahan AA, Roche K, Barnes CA, Huganir RL, Worley PF. Homer, a novel PDZ domain protein selectively binds PI-linked metabotropic glutamate receptors. Nature. 386:1997;284-288 Using two-hybrid system and in vitro biochemical assays, the authors show that Homer, a novel dendritic protein, interacts with metabotropic glutamate receptors mGluR-1 and mGluR-5. The carboxy-terminal sequence SSSS/TL in mGluR-1 and mGluR-5 is critical for the binding. Homer contains a PDZ domain and is the product of an immediate early gene that is dynamically regulated by different forms of neuronal activity. of outstanding interest.
23. Songyang Z, Fanning AS, Fu C, Xu J, Marfatia SM, Chishti AH, Crompton A, Chan AC, Anderson JM, Cantley LC. Recognition of unique carboxy-terminal motifs by distinct PDZ domains. Science. 275:1997;73-77 The specificities of nine PDZ domains were investigated by an oriented peptide library technique. Comparing the optimal motifs selected by the PDZ domains, two families of PDZ domains could be distinguished. One recognized the sequence ES/TXV/I* and the other selected peptides with three hydrophobic or aromatic sidechains at the carboxyl terminus. The specificities could be rationalized on the basis of the crystal structure of PDZ3 from PSD-95. of outstanding interest.
24. + channel Kir2.3, which contains a PKA consensus site in the terminal sequence RRESAI*, they could show in a heterologous cell system that phosphorylation of the serine occurs after activation of PKA. Interestingly, this tSXV-related sequence can be bound by PSD-95 and the binding is inhibited by phosphorylation of the serine at the -2 position. of special interest.
25. Hata Y, Butz S, Südhof TC. CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins. J Neurosci. 16:1996;2488-2494 This study describes the cloning and characterization of a novel protein termed CASK. This hybrid between a CAM kinase and a MAGUK protein is shown to bind to the carboxyl terminus of certain neurexins by the two-hybrid system and an in vitro biochemical assay. of special interest.
26. Simske JS, Kaech SM, Harp SA, Kim SK. LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction. Cell. 85:1996;195-204 These authors gained insight into the functional consequences of a PDZ domain interaction in C. elegans. They showed that the LIN-7 protein, which contains one PDZ domain, interacts with the receptor tyrosine kinase LET-23 at vulval precursor cell junctions. In lin-7 mutant worms, the LET-23 receptor is mislocalized, resulting in a vulvaless phenotype. These data provided the first in vivo evidence that a PDZ domain interaction functions in localizing a receptor protein. Interestingly, overexpression of LET-23 rescued the vulva-less phenotype. of special interest.
27. Apperson ML, Moon IS, Kennedy MB. Characterization of densin-180, a new brain-specific synaptic protein of the O-sialoglycoprotein family. J Neurosci. 16:1996;6839-6852 The purification and cloning of a novel component of the postsynaptic density of rat forebrain, densin-180, is described here. The primary sequence revealed leucine-rich repeats, a highly glycosylated rod-like structure, a transmembrane domain and a PDZ domain. The domain arrangement of densin-180 resembles that of adhesion molecules, such as the platelet glycoprotein (GP)-Ibα. of special interest.
28. Hunt CA, Schenker LJ, Kennedy MB. PSD-95 is associated with the postsynaptic density of forebrain synapses. J Neurosci. 16:1996;1380-1388.
29. Brenman JE, Chao DS, Gee SH, McGee AW, Craven SE, Santanillo DR, Wu Z, Huang F, Xia H, Peters MF, et al. Interaction of nitric oxide synthase with postsynaptic density protein PSD-95 and α1-syntrophin mediated by PDZ domains. Cell. 84:1996;757-767 The authors show binding of nNOS to PSD-95, PSD-93 and α1-syntrophin by the two-hybrid system and in vitro biochemical assays. Interestingly, the binding is mediated by a novel PDZ - PDZ interaction with no involvement of a carboxy-terminal peptide. of special interest.
30. Huang PL, Dawson TM, Bredt DS, Snyder SH, Fishman MC. Targeted disruption of the neuronal nitric oxide synthase gene. Cell. 75:1993;1273-1286.
31. Lahey T, Gorcyca M, Jia X-X, Budnik V. The Drosophila tumor suppressor gene dlg is required for normal synaptic bouton structure. Neuron. 13:1994;823-835.
32. Guan B, Hartmann B, Kho Y-H, Gorczyca M, Budnik V. The Drosophila tumor suppressor gene, dlg, is involved in structural plasticity at a glutamatergic synapse. Curr Biol. 6:1996;695-706.
33. + channel clusters at glutamatergic synapses of neuromuscular junctions in both dlg and shaker mutant flies. A deletion mutant lacking the tSXV motif of shaker and a subset of the various dlg mutants abolished the synaptic clustering. The results from the dlg mutants suggest that channel clustering and synaptic targeting depend on distinct domains in Dlg. This study provides in vivo evidence for a role in channel clustering of PDZ1 and PDZ2 of Dlg. of outstanding interest.
34. 2+-dependent currents. of special interest.
35. 2+ channel to a signal transduction complex containing phospholipase C-β, rhodopsin and calmodulin. of special interest.