Extracellular signal-regulated kinase (ERK) activity during sleep consolidates cortical plasticity in vivo

Michelle C Dumoulin; Sara J Aton; Adam J Watson; Leslie Renouard; Tammi Coleman; Marcos G Frank

doi:10.1093/cercor/bht250

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Extracellular signal-regulated kinase (ERK) activity during sleep consolidates cortical plasticity in vivo

Journal article

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Extracellular signal-regulated kinase (ERK) activity during sleep consolidates cortical plasticity in vivo

Michelle C Dumoulin, Sara J Aton, Adam J Watson, Leslie Renouard, Tammi Coleman and Marcos G Frank

Cerebral cortex (New York, N.Y. 1991), Vol.25(2), pp.507-515

02/2015

DOI: https://doi.org/10.1093/cercor/bht250

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https://hdl.handle.net/2376/107342

PMCID: PMC4303804

PMID: 24047601

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Abstract

Dominance, Ocular - physiology

Nitriles - pharmacology

Eukaryotic Initiation Factor-4E - metabolism

Neuronal Plasticity - drug effects

Male

Extracellular Signal-Regulated MAP Kinases - metabolism

Neuronal Plasticity - physiology

Dominance, Ocular - drug effects

Female

Phosphorylation - drug effects

Sleep - physiology

MAP Kinase Kinase Kinases - antagonists & inhibitors

Neurons - drug effects

Action Potentials - drug effects

Butadienes - pharmacology

Cats

Aniline Compounds - pharmacology

Purines - pharmacology

MAP Kinase Kinase Kinases - metabolism

Sleep - drug effects

Visual Cortex - enzymology

Sensory Deprivation - physiology

Animals

Neurons - enzymology

Protein Kinase Inhibitors - pharmacology

Visual Cortex - drug effects

Ocular dominance plasticity (ODP) in the cat primary visual cortex (V1) is induced during waking by monocular deprivation (MD) and consolidated during subsequent sleep. The mechanisms underlying this process are incompletely understood. Extracellular signal-regulated kinase (ERK) is activated in V1 during sleep after MD, but it is unknown whether ERK activation during sleep is necessary for ODP consolidation. We investigated the role of ERK in sleep-dependent ODP consolidation by inhibiting the ERK-activating enzyme MEK in V1 (via U0126) during post-MD sleep. ODP consolidation was then measured with extracellular microelectrode recordings. Western blot analysis was used to confirm the efficacy of U0126 and to examine proteins downstream of ERK. U0126 abolished ODP consolidation and reduced both phosphorylation of eukaryotic initiation factor 4E (eIF4E) and levels of the synaptic marker PSD-95. Furthermore, interfering with ERK-mediated translation by inhibiting MAP kinase-interacting kinase 1 (Mnk1) with CGP57380 mimicked the effects of U0126. These results demonstrate that ODP consolidation requires sleep-dependent activation of the ERK-Mnk1 pathway.

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Title: Extracellular signal-regulated kinase (ERK) activity during sleep consolidates cortical plasticity in vivo
Creators: Michelle C Dumoulin - Department of Neuroscience, School of Medicine, University of Pennsylvania, Philadelphia, PA
Sara J Aton - Department of Neuroscience, School of Medicine, University of Pennsylvania, Philadelphia, PA
Adam J Watson - Department of Neuroscience, School of Medicine, University of Pennsylvania, Philadelphia, PA
Leslie Renouard - Department of Neuroscience, School of Medicine, University of Pennsylvania, Philadelphia, PA
Tammi Coleman - Department of Neuroscience, School of Medicine, University of Pennsylvania, Philadelphia, PA
Marcos G Frank - Department of Neuroscience, School of Medicine, University of Pennsylvania, Philadelphia, PA
Publication Details: Cerebral cortex (New York, N.Y. 1991), Vol.25(2), pp.507-515
Academic Unit: Biomedical Sciences, Department of
Publisher: United States
Grant note: T32 EY007143 / NEI NIH HHS K99 EY021503 / NEI NIH HHS R01 EY019022 / NEI NIH HHS R01 HL114161 / NHLBI NIH HHS F32 EY006831 / NEI NIH HHS F32 EY017766 / NEI NIH HHS HL114161 / NHLBI NIH HHS T32 GM007517 / NIGMS NIH HHS F31NS067935 / NINDS NIH HHS T32 HL007953 / NHLBI NIH HHS EY019022 / NEI NIH HHS R00 EY021503 / NEI NIH HHS
Identifiers: 99900547139901842
Language: English
Resource Type: Journal article