ArticleThe Journal of biological chemistry2017
Src homology 2 domain-containing phosphotyrosine phosphatase 2 (Shp2) controls surface GluA1 protein in synaptic homeostasis.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Targeting Shp2 as a therapeutic strategy for neurodegenerative diseases.Translational psychiatry · 2025Review
- SHP2 regulates GluA2 tyrosine phosphorylation required for AMPA receptor endocytosis and mGluR-LTD.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cathepsin K inhibition induces Raptor destabilization and mitochondrial dysfunction via Syk/SHP2/Src/OTUB1 axis-mediated signaling.Cell death & disease · 2023Article
- Strategies to overcome drug resistance using SHP2 inhibitors.Acta pharmaceutica Sinica. B · 2021Review
- The Noonan syndrome-associated D61G variant of the protein tyrosine phosphatase SHP2 prevents synaptic down-scaling.The Journal of biological chemistry · 2020Article
- De novo damaging variants associated with congenital heart diseases contribute to the connectome.Scientific reports · 2020Article
- Connecting the dots between SHP2 and glutamate receptors.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2020Review
- Excitatory neuron-specific SHP2-ERK signaling network regulates synaptic plasticity and memory.Science signaling · 2019Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Src Homology 2 domain-containing phosphotyrosine phosphatase 2 (Shp2) functions in synaptic plasticity, learning, and memory. However, the precise mechanisms by which this multifunctional protein contributes to synaptic function remains largely unknown. Homeostatic plasticity may be viewed as a process of bidirectional synaptic scaling, up or down. Through this process, neuronal circuitry stability is maintained so that changes in synaptic strength may be preserved under changing conditions. A better understanding of these processes is needed. In this regard, we report that phosphorylation of Shp2 at tyrosine 542 and its translocation to the postsynaptic compartment are integral processes in synaptic scaling. Furthermore, we show, using both pharmacological and genetic approaches, that Shp2 phosphatase activity is critical to the regulation of Ser(P)
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Registered trials
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