Cysteine regulation of protein function - As exemplified by NMDA-receptor modulation

Trends in Neurosciences

Volumn 25, Issue 9, 2002, Pages 474-480

  Lipton, Stuart A ^a   Choi, Yun Beom ^a   Takahashi, Hiroto ^a   Zhang, Dongxian ^a   Li, Weizhong ^a   Godzik, Adam ^a   Bankston, Laurie A ^a  

^a BURNHAM INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ION; CYSTEINE; MANGANESE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NITRIC OXIDE; THIOL DERIVATIVE; ZINC;

CATALYSIS; CHELATION; CHEMICAL MODIFICATION; CRYSTAL STRUCTURE; DISULFIDE BOND; LIGAND BINDING; MOLECULAR MODEL; NEUROMODULATION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; RECEPTOR DOWN REGULATION; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; CYSTEINE; HUMANS; MODELS, MOLECULAR; NITRIC OXIDE; OXIDATION-REDUCTION; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, N-METHYL-D-ASPARTATE; S-NITROSOTHIOLS; SULFHYDRYL COMPOUNDS;

EID: 0036752945     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-2236(02)02245-2     Document Type: Review

References (40)

1. Lipton S.A., et al. A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds. Nature. 364:1993;626-632.
2. Stamler J.S. Redox signaling: nitrosylation and related target interactions of nitric oxide. Cell. 78:1994;931-936.
3. Stamler J.S., et al. (S)NO signals: translocation, regulation and a consensus motif. Neuron. 18:1997;691-696.
4. Katzen F., Beckwith J. Transmembrane electron transfer by the membrane protein CsbD occurs via disulfide bond cascade. Cell. 103:2000;769-779.
5. Lay A.J., et al. Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase. Nature. 408:2000;869-873.
6. Gergel D., Cederbaum A.I. Inhibition of the catalytic activity of alcohol dehydrogenase by nitric oxide is associated with S-nitrosylation and the release of zinc. Biochemistry. 35:1996;16186-16194.
7. Kroncke K.D., Carlberg C. Inactivation of zinc finger transcription factors provides a mechanism for a gene regulatory role of nitric oxide. FASEB J. 14:2000;166-173.
8. Choi H., et al. Structural basis of the redox switch in the OxyR transcription factor. Cell. 105:2001;103-113.
9. Kroncke K.D., et al. Nitric oxide destroys zinc-sulfur clusters inducing zinc release from metallothionein and inhibition of the zinc finger-type yeast transcription activator LAC9. Biochem. Biophys. Res. Commun. 200:1994;1105-1110.
10. Misra R.R., et al. Evidence that nitric oxide enhances cadmium toxicity by displacing the metal from metallothionein. Chem. Res. Toxicol. 9:1996;326-332.
11. 2+ release from metallothionein by destroying zinc-sulphur clusters without concomitant formation of S-nitrosothiol. Biochem. J. 344:1999;253-258.
12. Pearce L.L., et al. Role of metallothionein in nitric oxide signaling as revealed by a green fluorescent fusion protein. Proc. Natl. Acad. Sci. U. S. A. 97:2000;477-482.
13. Stamler J.S., et al. Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient. Science. 276:1997;2034-2037.
14. Broillet M.-C. A single intracellular cysteine residue is responsible for the activation of the olfactory cyclic nucleotide-gated channel by NO. J. Biol. Chem. 275:2000;15135-15141.
15. Lei S.Z., et al. Effect of nitric oxide production on the redox modulatory site of the NMDA receptor-channel complex. Neuron. 8:1992;1087-1099.
16. -). Neuron. 24:1999;461-469.
17. Choi Y.-B., et al. Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation. Nat. Neurosci. 3:2000;15-21.
18. 2+ modulation of the NMDA receptor. J. Neurosci. 21:2001;392-400.
19. Paoletti P., et al. Molecular organization of a zinc binding N-terminal modulatory domain in a NMDA receptor subunit. Neuron. 28:2000;911-925.
20. + channels in C-type DRG neurons by S-nitrosylation. J. Neurophysiol. 87:2002;761-775.
21. Lipton S.A., Rosenberg R.A. Mechanisms of disease: Excitatory amino acids as a final common pathway in neurologic disorders. New Engl. J. Med. 330:1994;613-622.
22. McBain C.J., Mayer M.L. N-methyl-D-aspartic acid receptor structure and function. Physiol. Rev. 74:1994;723-760.
23. Sucher N.J., et al. NMDA receptors: from genes to channels. Trends Pharmacol. Sci. 17:1996;348-355.
24. Sullivan J.M., et al. Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor. Neuron. 13:1994;929-936.
25. Armstrong N., et al. Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature. 395:1998;913-917.
26. Masuko T., et al. A regulatory domain (R1-R2) in the amino terminus of the N-methyl-D-aspartate receptor: effects of spermine, protons, and ifenprodil, and structural similarity to bacterial leucine/isoleucine/valine binding protein. Mol. Pharmacol. 55:1999;957-969.
27. Kunishima N., et al. Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Nature. 407:2000;971-977.
28. 2+ inhibition of the NMDA receptor. Neuron. 23:1999;171-180.
29. 2+ binding to NMDA receptors. Neuron. 25:2000;683-694.
30. Low C.-M., et al. Molecular determinants of coordinated proton and zinc inhibition of N-methyl-D-aspartate NR1/NR2A receptors. Proc. Natl. Acad. Sci. U. S. A. 97:2000;11062-11067.
31. Stamler J.S., et al. Biochemistry of nitric oxide and its redox-activated forms. Science. 258:1992;1898-1902.
32. Zheng F., et al. Allosteric interaction between the amino terminal domain and the ligand binding domain of NR2A. Nat. Neurosci. 4:2001;894-901.
33. Stern-Bach Y., et al. Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins. Neuron. 13:1994;1345-1357.
34. Wo Z.G., Oswald R.E. Unraveling the modular design of glutamate-gated ion channels. Trends Neurosci. 18:1995;161-168.
35. Sack J.S., et al. Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine. J. Mol. Biol. 206:1989;171-191.
36. Armstrong N., Gouaux E. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron. 28:2000;165-181.
37. Chen N., et al. Differential sensitivity of recombinant N-methyl-D-aspartate receptor subtypes to zinc inhibition. Mol. Pharmacol. 51:1997;1015-1023.
38. Paoletti P., et al. High-affinity zinc inhibition of NMDA NR1-NR2A receptors. J. Neurosci. 17:1997;5711-5725.
39. Sun Y., et al. Mechanism of glutamate receptor desensitization. Nature. 417:2002;245-253.
40. Traynelis S.F., et al. Control of proton sensitivity of the NMDA receptor by RNA splicing and polyamines. Science. 268:1995;873-876.