Requirement of JIP scaffold proteins for NMDA-mediated signal transduction
Open accessAbstract
JIP scaffold proteins are implicated in the regulation of protein kinase signal transduction pathways. To test the physiological role of these scaffold proteins, we examined the phenotype of compound mutant mice that lack expression of JIP proteins. These mice were found to exhibit severe defects in N-methyl-D-aspartic acid (NMDA) receptor function, including decreased NMDA-evoked current amplitude, cytoplasmic Ca++, and gene expression. The decreased NMDA receptor activity in JIP-deficient neurons is associated with reduced tyrosine phosphorylation of NR2 subunits of the NMDA receptor. JIP complexes interact with the SH2 domain of cFyn and may therefore promote tyrosine phosphorylation and activity of the NMDA receptor. We conclude that JIP scaffold proteins are critically required for normal NMDA receptor function.
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JIP is localized at post-synaptic densities (PSD) in neurons and is indispensable for normal function of NMDA receptors.
“Recent studies have shown that JIP is localized at post-synaptic densities (PSD) in neurons, and is indispensable for the normal function of NMDA receptors (Kennedy et al., 2007; Pellet et al., 2000).”
From The E3 ubiquitin ligase IDOL regulates synaptic ApoER2 levels and is important for plasticity and learning (2017) · cites this paper as Kennedy et al., 2007
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Cites
A Mammalian Scaffold Complex That Selectively Mediates MAP Kinase Activation
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The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and -2
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“Indeed, several ligands for this PTB domain have been described, including the low-density lipoprotein receptor-related protein LRP8 (Stockinger et al. 2000), the Rac exchange factor Tiam1 (Buchsbaum et al. 2002), and the Ras exchange factor Ras-Grf (Buchsbaum et al. 2002).”
BackgroundInfluentialAn essential role of the JIP1 scaffold protein for JNK activation in adipose tissue
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Behavioral and Cerebellar Transmission Deficits in Mice Lacking the Autism-Linked Gene Islet Brain-2
Giza, J., Urbanski, M. J., Prestori, F., Bandyopadhyay, B., Yam, A., Friedrich, V., Kelley, K., D'Angelo, E., & Goldfarb, M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.1161-10.2010 · Cited by 68 · see citing works
Morel, C., Standen, C. L., Jung, D. Y., Gray, S., Ong, H., Flavell, R. A., Kim, J. K., & Davis, R. J. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00585-10 · Cited by 30 · see citing works
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- Authors
- Kennedy, N. J., Martin, G., Ehrhardt, A. G., Cavanagh-Kyros, J., Kuan, C.-Y., Rakic, P., Flavell, R. A., Treistman, S. N., & Davis, R. J.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of Massachusetts Chan Medical School (US)
- Cincinnati Children's Hospital Medical Center (US)
- Yale University (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2007-09-15
- Volume
- 21
- Issue
- 18
- Pages
- 2336-2346
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC1973147
- OpenAlex
- W2035613198
- Cited by
- 40
- References
- 4
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 2 · 2017: 5 · 2016: 1 · 2015: 4 · 2014: 2 · 2013: 2 · 2012: 1
- Type
- posted content
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- other-oa
- Locations
- Genes & Development (publishedVersion, other-oa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship@UMassChan (submittedVersion, other-oa)
- Funders
- Howard Hughes Medical Institute
- Charles A. King Trust
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-52530, R01DK052530)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- NMDA receptor, signal transduction, SH2 domain, calcium signaling, compound mutant mice, synaptic transmission
- MeSH terms
- Animals, Chlorocebus aethiops, Cerebellum, Mice, Inbred C57BL, Neurons, Phosphorylation, Protein-Tyrosine Kinases, Signal Transduction, Receptors, N-Methyl-D-Aspartate, N-Methylaspartate, Kinesins, Mice, Knockout, COS Cells, Adaptor Proteins, Signal Transducing, Mice
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