Proteomics of the Synapse – A Quantitative Approach to Neuronal Plasticity

Dieterich, Daniela C.; Kreutz, Michael R.

doi:10.1074/mcp.r115.051482

Cited by 63 publications

(58 citation statements)

References 200 publications

(154 reference statements)

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“…Additionally, in a moderate number of O-GlcNAc-ylation sites, there is a proline two or three resides towards the amino-terminal or, less frequently, a valine one or three residues amino-terminal. Previously, PVXS/T had been suggested as a possible O-GlcNAc-ylation motif, however, this motif occurred at less than 20% of all identified sites 10,11 . The above results might suggest the absence of a universally consensus motif 1,12 .…”

Section: O-glcnac Is a Universal Post-translation Modification In Allmentioning

confidence: 90%

O-GlcNAc-ylation in the Nuclear Pore Complex

Ruba

Yang

2016

Cel. Mol. Bioeng.

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O-GlcNAc-ylation is the post-translational addition of an O-linked β-N-acetylglucosamine to the serine and threonine residues of thousands of proteins in eukaryotic cells. Specifically, half of the thirty different types of protein components in the nuclear pore complex (NPC) are modified by O-GlcNAc, of which the majority are intrinsically disordered nucleoporins (Nups) containing multiple phenylalanine-glycine (FG) repeats. Moreover, these FG-Nups form a strict selectivity barrier with a high density of O-GlcNAc in the NPC to mediate bidirectional trafficking between the cytoplasm and nucleus. However, the roles that O-GlcNAc plays in the structure and function of the NPC remain obscure. In this review paper, we will discuss the current knowledge of O-GlcNAc-ylated Nups, highlight some new techniques used to probe O-GlcNAc's roles in the nuclear pore, and finally propose a new model for the effect of O-GlcNAc on the NPC's permeability.

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Section: O-glcnac Is a Universal Post-translation Modification In Allmentioning

confidence: 90%

O-GlcNAc-ylation in the Nuclear Pore Complex

Ruba

Yang

2016

Cel. Mol. Bioeng.

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“…The advances in mass spectrometry (MS)-based large-scale proteomics and phosphoproteomics have enabled the identification and quantification of hundreds to more than 2,000 PSD proteins and their posttranslational modifications [1–7]. These studies unraveled not only the postsynaptic organization of synapses, but also the signaling networks driven by neurotransmitter receptor activation [8,9]. They greatly enhanced our understanding of synaptic plasticity and related neurodegenerative or psychiatric disorders.…”

Section: Introductionmentioning

confidence: 99%

Proteomic Analysis of Mouse Cortex Postsynaptic Density following Neonatal Brain Hypoxia-Ischemia

Shao

Wang²,

Guan³

et al. 2017

Dev Neurosci

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Proteomics of the synapses and postsynaptic densities (PSDs) have provided a deep understanding of protein composition and signal networks in the adult brain, which underlie neuronal plasticity and neurodegenerative or psychiatric disorders. However, there is a paucity of knowledge about the architecture and organization of PSDs in the immature brain, and how it is modified by brain injury in an early developing stage. Mass spectrometry (MS)-based proteomic analysis was performed on PSDs prepared from cortices of postnatal day 9 naïve mice or pups which had suffered hypoxic-ischemic (HI) brain injury. 512 proteins of different functional groups were identified from PSDs collected 1 h after HI injury, among which 60 have not been reported previously. Seven newly identified proteins involved in neural development were highlighted. HI injury increased the yield of PSDs at early time points upon reperfusion, and multiple proteins were recruited into PSDs following the insult. Quantitative analysis was performed using spectral counting, and proteins whose relative expression was more than 50% up- or downregulated compared to the sham animals 1 h after HI insult were reported. Validation with Western blotting demonstrated changes in expression and phosphorylation of the N-methyl-D-aspartate receptor, activation of a series of postsynaptic protein kinases and dysregulation of scaffold and adaptor proteins in response to neonatal HI insult. This work, along with other recent studies of synaptic protein profiling in the immature brain, builds a foundation for future investigation on the molecular mechanisms underlying developing plasticity. Furthermore, it provides insights into the biochemical changes of PSDs following early brain hypoxia-ischemia, which is helpful for understanding not only the injury mechanisms, but also the process of repair or replenishment of neuronal circuits during recovery from brain damage.

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“…Moreover, chemical synapses can be divided into two types: excitatory and inhibitory [40][41][42][43]. Chemical synapses, which are the most common type of cellular connections in the animal's nervous system, are highly flexible, making this topic widely studied [44][45][46].…”

Section: Synchronization Of the Chemical Synaptic-coupled Chay Neuronmentioning

confidence: 99%

Synchronization of Chemical Synaptic Coupling of the Chay Neuron System under Time Delay

Wang

et al. 2018

Applied Sciences

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This paper studies the chemical synaptic coupling of Chay neurons and the effect of adding time delay on their synchronization behavior. The results indicate that coupling strength stimuli can affect the discharge activity and the synchronization behavior. In the absence of coupling strength, the Chay neurons have chaotic discharge behavior and the system is in a nonsynchronous state. When a certain coupling strength is added, the neurons change from chaotic discharge to ordered periodic discharge, and the system state changes from asynchronous to synchronous. On the other hand, a time lag can alter the coupled system from synchronous to asynchronous.

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Proteomics of the Synapse – A Quantitative Approach to Neuronal Plasticity

Cited by 63 publications

References 200 publications

O-GlcNAc-ylation in the Nuclear Pore Complex

O-GlcNAc-ylation in the Nuclear Pore Complex

Proteomic Analysis of Mouse Cortex Postsynaptic Density following Neonatal Brain Hypoxia-Ischemia

Synchronization of Chemical Synaptic Coupling of the Chay Neuron System under Time Delay

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