S-Nitrosylation of N-Ethylmaleimide Sensitive Factor Mediates Surface Expression of AMPA Receptors

Huang, Yunfei; Man, Heng Ye; Sekine‐Aizawa, Yoko; Han, Yefei; Juluri, Krishna R.; Luo, Hongbo; Cheah, Jaime H.; Lowenstein, Charles J.; Huganir, Richard L.; Snyder, Solomon H.

doi:10.1016/j.neuron.2005.03.028

Cited by 165 publications

(153 citation statements)

References 41 publications

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“…A single Cys is contained in 53 of these peptides, defining the site of S-nitrosylation; for the remaining five peptides, it remains to be shown which of two alternative Cys residues are S-nitrosylation sites. (20) and upregulation of ␣-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor expression (21). Together, the cerebellar SNO peptides listed in Table 1 are consistent with broad-reaching functions for SNO proteins in neuroregulation and provide a road map for Cys residues that may subserve pivotal roles in transducing NO bioactivities in brain.…”

Section: Identification Of Sno-cys By Nlc-ms͞ms and Database Searchingmentioning

confidence: 58%

SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures

Hao

Derakhshan

Shi

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

316

320

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Reversible addition of NO to Cys-sulfur in proteins, a modification termed S-nitrosylation, has emerged as a ubiquitous signaling mechanism for regulating diverse cellular processes. A key first-step toward elucidating the mechanism by which S-nitrosylation modulates a protein's function is specification of the targeted Cys (SNO-Cys) residue. To date, S-nitrosylation site specification has been laboriously tackled on a protein-by-protein basis. Here we describe a high-throughput proteomic approach that enables simultaneous identification of SNO-Cys sites and their cognate proteins in complex biological mixtures. The approach, termed SNOSID (SNO Site Identification), is a modification of the biotin-swap technique [Jaffrey, S. R., Erdjument-Bromage, H., Ferris, C. D., Tempst, P. & Snyder, S. H. (2001) Nat. Cell. Biol. 3, 193–197], comprising biotinylation of protein SNO-Cys residues, trypsinolysis, affinity purification of biotinylated-peptides, and amino acid sequencing by liquid chromatography tandem MS. With this approach, 68 SNO-Cys sites were specified on 56 distinct proteins in S -nitrosoglutathione-treated (2–10 μM) rat cerebellum lysates. In addition to enumerating these S-nitrosylation sites, the method revealed endogenous SNO-Cys modification sites on cerebellum proteins, including α-tubulin, β-tubulin, GAPDH, and dihydropyrimidinase-related protein-2. Whereas these endogenous SNO proteins were previously recognized, we extend prior knowledge by specifying the SNO-Cys modification sites. Considering all 68 SNO-Cys sites identified, a machine learning approach failed to reveal a linear Cys-flanking motif that predicts stable transnitrosation by S -nitrosoglutathione under test conditions, suggesting that undefined 3D structural features determine S-nitrosylation specificity. SNOSID provides the first effective tool for unbiased elucidation of the SNO proteome, identifying Cys residues that undergo reversible S-nitrosylation.

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Section: Identification Of Sno-cys By Nlc-ms͞ms and Database Searchingmentioning

confidence: 58%

SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures

Hao

Derakhshan

Shi

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

316

320

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“…It is important to note that NO signalling by guanylate cyclase and S-nitrosylation are not necessarily mutually exclusive [12,13]. S-nitrosylation has been implicated in transmitting signals downstream of all classes of receptors, including GPCRs, RTKs, TNF, Toll, glutaminergic and other [1,[14][15][16]--acting locally within subcellular signaling domains as well conveying signals from the cell surface to intracellular compartments, including the mitrochondria and the nucleus (e.g. by modification of transcription factors).…”

Section: Oxidants As Modulators Of Signal Transductionmentioning

confidence: 99%

“…Indeed, a number of targets such as caspases, receptors (e.g. alpha-amino-3-hydroxy-5-methylisoxasole-4-propionic acid (AMPA) and NMDA), kinases, G proteins and ion channels have been demonstrated to be S-nitrosylated under physiological conditions [15,53,54]. In diverse cell types, S-nitrosylation can be detected in situ under both non-stimulated conditions and following physiological activation (e.g stimulation of GPCRs to dilate blood vessels or stimulate cardiac contractility [55,56]).…”

Section: Relative Importance Of No-or H 2 O 2 -Dependent Cysteine Oximentioning

confidence: 99%

“…Furthermore, as will be described below, regulatory enzymes important in redox control, such as thioredoxin, glutaredoxin, peroxiredoxin, and protein disulfide isomerase, are themselves affected and regulated by both H 2 O 2 and NO-based cysteine oxidations. It is of interest to note that S-nitrosylation may be criticaly sensitive to oxygen tension, often being potentiated by hypoxia [15,54,57]. Further, it has been shown that oxidation/reduction (of a group) of thiols may regulate S-nitrosylation by an allosteric mechanism [57].…”

Section: Relative Importance Of No-or H 2 O 2 -Dependent Cysteine Oximentioning

confidence: 99%

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Redox-based regulation of signal transduction: Principles, pitfalls, and promises

Janssen–Heininger¹,

Mossman²,

Heintz³

et al. 2008

Free Radical Biology and Medicine

698

652

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“…Intriguingly, NSF also plays a vital role at the postsynaptic membrane and is necessary for plasma membrane insertion of GluA2-containing AMPARs, increasing its surface expression (Huang et al, 2005;Araki et al, 2010). NSF binds the GluA2 C-terminus upstream of the PDZ binding site between residues Lys844 and Gln853.…”

Section: Introductionmentioning

confidence: 99%

Presynaptic PICK1 facilitates trafficking of AMPA-receptors between active zone and synaptic vesicle pool

et al. 2017

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General rightsThis document is made available in accordance with publisher policies. Please cite only the published version using the reference above. AbstractPrevious studies have indicated that presynaptic -amino-3-hydroxy-5-methyl-4-isoxazole propionate receptors (AMPARs) contribute to the regulation of neurotransmitter release. In hippocampal synapses, the presynaptic surface expression of several AMPAR subunits, including GluA2, is regulated in a ligand dependent manner. However, the molecular mechanisms underlying the presynaptic trafficking of AMPARs are still unknown. Here, using bright-field immunocytochemistry, western blots, and quantitative immunogold electron microscopy of the hippocampal CA1 area from intact adult rat brain, we demonstrate the association of AMPA receptors with the presynaptic active zone and with small presynaptic vesicles, in Schaffer collateral synapses in CA1 of the hippocampus. Furthermore, we show that GluA2 and protein interacting with C kinase 1 (PICK1) are colocalized at presynaptic vesicles. Similar to postsynaptic mechanisms, overexpression of either PICK1 or pep2m, which inhibit the N-ethylmaleimide sensitive fusion protein (NSF)-GluA2 interaction, decreases the concentration of GluA2 in the presynaptic active zone membrane. These data suggest that the interacting proteins PICK1 and NSF act as regulators of presynaptic GluA2-containing AMPAR trafficking between the active zone and a vesicle pool that may provide the basis of presynaptic components of synaptic plasticity.

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S-Nitrosylation of N-Ethylmaleimide Sensitive Factor Mediates Surface Expression of AMPA Receptors

Cited by 165 publications

References 41 publications

SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures

SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures

Redox-based regulation of signal transduction: Principles, pitfalls, and promises

Presynaptic PICK1 facilitates trafficking of AMPA-receptors between active zone and synaptic vesicle pool

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