ArticleScientific reports2015
Presynaptic c-Jun N-terminal Kinase 2 regulates NMDA receptor-dependent glutamate release.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
32 citing papers in PubMed, 56 citations in OpenAlex.
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- Presynaptic release-regulating NMDA receptors in isolated nerve terminals: A narrative review.British journal of pharmacology · 2021Review
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- Involvement of homodomain interacting protein kinase 2-c-Jun N-terminal kinase/c-Jun cascade in the long-term synaptic toxicity and cognition impairment induced by neonatal Sevoflurane exposure.Journal of neurochemistry · 2020Article
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- The selective disruption of presynaptic JNK2/STX1a interaction reduces NMDA receptor-dependent glutamate release.Scientific reports · 2019Article
- The Involvement of Peripheral and Brain Insulin Resistance in Late Onset Alzheimer's Dementia.Frontiers in aging neuroscience · 2019Article
- Mitogen-activated protein kinase signaling mediates opioid-induced presynaptic NMDA receptor activation and analgesic tolerance.Journal of neurochemistry · 2019Article
- NLRP3-Dependent and -Independent Processing of Interleukin (IL)-1β in Active Ulcerative Colitis.International journal of molecular sciences · 2018Article
- Role of Mitogen Activated Protein Kinase Signaling in Parkinson's Disease.International journal of molecular sciences · 2018Review
- Unconventional NMDA Receptor Signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Review
Corrections and comments
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Authors and funding
15 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Activation of c-Jun N-terminal kinase (JNK) signaling pathway is a critical step for neuronal death occurring in several neurological conditions. JNKs can be activated via receptor tyrosine kinases, cytokine receptors, G-protein coupled receptors and ligand-gated ion channels, including the NMDA glutamate receptors. While JNK has been generally associated with postsynaptic NMDA receptors, its presynaptic role remains largely unexplored. Here, by means of biochemical, morphological and functional approaches, we demonstrate that JNK and its scaffold protein JIP1 are also expressed at the presynaptic level and that the NMDA-evoked glutamate release is controlled by presynaptic JNK-JIP1 interaction. Moreover, using knockout mice for single JNK isoforms, we proved that JNK2 is the essential isoform in mediating this presynaptic event. Overall the present findings unveil a novel JNK2 localization and function, which is likely to play a role in different physiological and pathological conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.