PSD-95 stabilizes NMDA receptors by inducing the degradation of STEP 61 | Zendy

Sehoon Won | Zendy; Salvatore Incontro | Zendy; Roger A. Nicoll | Zendy; Katherine W. Roche | Zendy

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PSD-95 stabilizes NMDA receptors by inducing the degradation of STEP ₆₁

Author(s) -

Sehoon Won,

Salvatore Incontro,

Roger A. Nicoll,

Katherine W. Roche

Publication year - 2016

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.1609702113

Subject(s) - postsynaptic density , nmda receptor , phosphorylation , microbiology and biotechnology , tyrosine , gene knockdown , biology , signal transducing adaptor protein , dephosphorylation , scaffold protein , protein tyrosine phosphatase , chemistry , phosphatase , biochemistry , biophysics , receptor , signal transduction , apoptosis

Significance NMDA receptors (NMDARs) are principal regulators of synaptic signaling in the brain. Modulation of NMDARs’ function and trafficking is important for the regulation of synaptic transmission and several forms of synaptic plasticity. Postsynaptic density protein 95 (PSD-95) acts as a scaffolding protein and stabilizes the surface and synaptic expression of NMDARs, whereas striatal-enriched protein tyrosine phosphatase (STEP), a brain-specific protein tyrosine phosphatase, dephosphorylates and destabilizes NMDARs via endocytosis. We now demonstrate that PSD-95 binds to STEP61 and promotes its degradation via the proteasome, thereby stabilizing surface expression of NMDARs. We have revealed a dynamic role for PSD-95 in sculpting protein content at excitatory synapses that is distinct from its canonical role as a scaffolding protein.

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