Mitogen-activated protein kinase signaling is essential for activity-dependent dendritic protein synthesis

Gong, Ruomu; Tang, Shao-Jun

doi:10.1097/01.wnr.0000234742.42818.ff

Cited by 16 publications

(12 citation statements)

References 24 publications

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“…Interestingly, translational activation initiated by ERK signalling seems to be crucial in the control of cell-wide and somatodendritic protein synthesis underlying the stabilization of the late phases of synaptic plasticity and memory formation [52], [53]. The presence of pERK-immunolabelling on the external face of the RER (Fig 2A,B) is in agreement with a role of ERK in protein synthesis processes occurring in neurons.…”

Section: Discussionsupporting

confidence: 70%

Visual Stimulation Activates ERK in Synaptic and Somatic Compartments of Rat Cortical Neurons with Parallel Kinetics

et al. 2007

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BackgroundExtracellular signal-regulated kinase (ERK) signalling pathway plays a crucial role in regulating diverse neuronal processes, such as cell proliferation and differentiation, and long-term synaptic plasticity. However, a detailed understanding of the action of ERK in neurons is made difficult by the lack of knowledge about its subcellular localization in response to physiological stimuli. To address this issue, we have studied the effect of visual stimulation in vivo of dark-reared rats on the spatial-temporal dynamics of ERK activation in pyramidal neurons of the visual cortex.Methodology/Principal FindingsUsing immunogold electron microscopy, we show that phosphorylated ERK (pERK) is present in dendritic spines, both at synaptic and non-synaptic plasma membrane domains. Moreover, pERK is also detected in presynaptic axonal boutons forming connections with dendritic spines. Visual stimulation after dark rearing during the critical period causes a rapid increase in the number of pERK-labelled synapses in cortical layers I–II/III. This visually-induced activation of ERK at synaptic sites occurs in pre- and post-synaptic compartments and its temporal profile is identical to that of ERK activation in neuronal cell bodies.Conclusions/SignificanceVisual stimulation in vivo increases pERK expression at pre- and post-synaptic sites of axo-spinous junctions, suggesting that ERK plays an important role in the local modulation of synaptic function. The data presented here support a model in which pERK can have early and late actions both centrally in the cell nucleus and peripherally at synaptic contacts.

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Section: Discussionsupporting

confidence: 70%

Visual Stimulation Activates ERK in Synaptic and Somatic Compartments of Rat Cortical Neurons with Parallel Kinetics

et al. 2007

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“…Previous studies indicate that MAPK signaling is critical for activity-regulated protein synthesis in neurons [36,37]. We investigated the involvement of MAPK signaling in NMDAR-dependent Wnt5a protein synthesis using pharmacological approaches.…”

Section: Resultsmentioning

confidence: 99%

NMDA receptor activation stimulates transcription-independent rapid wnt5a protein synthesis via the MAPK signaling pathway

Wan

et al. 2012

Mol Brain

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Wnt proteins are emerging key regulators of the plasticity and functions of adult brains. However, the mechanisms by which the expression of Wnt proteins is regulated in neurons are unclear. Using cortical primary cultures, we show here that activation of NMDA receptors (NMDARs) induces rapid Wnt5a protein synthesis and secretion. This NMDAR-regulated Wnt5a synthesis does not require transcription and is a result of activity-dependent translation. We also show that NMDAR-regulated Wnt5a translation depends on MAPK signaling but not mTOR signaling. Our findings suggest that the synaptic activity of CNS neurons activates NMDARs, which in turn stimulate translation from stored Wnt5a mRNA via the MAPK signaling pathway.

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“…Activation of local MAPKs may accommodate the need of new protein synthesis at potentiated synapses for structural changes in relation to long-term synaptic plasticity. In support of this notion, an inducible dendritic protein synthesis was abolished by U0126 [53]. The studies on this topic are very limited.…”

Section: Discussionmentioning

confidence: 97%

Synaptically Localized Mitogen-Activated Protein Kinases: Local Substrates and Regulation

Mao

Wang

2015

Mol Neurobiol

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Mitogen-activated protein kinases (MAPKs) are expressed in postmitotic neurons and act as important regulators in intracellular signaling. In addition to their nuclear distribution and roles in regulating gene expression, MAPKs, especially the extracellular signal-regulated kinase (ERK) subclass, reside in peripheral dendritic spines and synapses, including the postsynaptic density (PSD) microdomain. This peripheral pool of MAPKs/ERKs is either constitutively active or sensitive to changing synaptic input. Active MAPKs directly interact with and phosphorylate local substrates to alter their trafficking and subcellular/subsynaptic distributions, through which MAPKs regulate function of substrates and contribute to long-lasting synaptic plasticity. A number of physiologically relevant substrates of MAPKs have been identified at synaptic sites. Central among them are key synaptic scaffold proteins (PSD-95 and PSD-93), cadherin-associated proteins (δ-catenin), Kv4.2 K+ channels, and metabotropic glutamate receptors. Through a reversible phosphorylation event, MAPKs rapidly and efficiently modulate the function of these substrates and thus determine the strength of synaptic transmission. This review summarizes the recent progress in cell biology of synaptic MAPKs and analyzes roles of this specific pool of MAPKs in regulating local substrates and synaptic plasticity.

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Mitogen-activated protein kinase signaling is essential for activity-dependent dendritic protein synthesis

Cited by 16 publications

References 24 publications

Visual Stimulation Activates ERK in Synaptic and Somatic Compartments of Rat Cortical Neurons with Parallel Kinetics

Visual Stimulation Activates ERK in Synaptic and Somatic Compartments of Rat Cortical Neurons with Parallel Kinetics

NMDA receptor activation stimulates transcription-independent rapid wnt5a protein synthesis via the MAPK signaling pathway

Synaptically Localized Mitogen-Activated Protein Kinases: Local Substrates and Regulation

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