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The Postsynaptic Density Protein PSD‐95 Differentially Regulates Insulin‐ and Src‐Mediated Current Modulation of Mouse NMDA Receptors Expressed in Xenopus Oocytes
Author(s) -
Liao GueyYing,
Kreitzer Matthew A.,
Sweetman Brian J.,
Leonard John P.
Publication year - 2000
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.2000.0750282.x
Subject(s) - long term potentiation , postsynaptic density , nmda receptor , biology , postsynaptic potential , microbiology and biotechnology , glutamatergic , receptor , proto oncogene tyrosine protein kinase src , glutamate receptor , kinase , biochemistry
: The NMDA subtype of glutamate receptor is physically associated with the postsynaptic density protein PSD‐95 at glutamatergic synapses. The channel activity of NMDA receptors is regulated by different signaling molecules, including protein tyrosine kinases. Because previous results have suggested a role for protein kinase C (PKC) in insulin potentiation of NMDA currents in oocytes, the effects of coexpression of PSD‐95 on insulin and PKC potentiation of NMDA currents from these receptors were compared. Another primary objective was to determine if PSD‐95 could enable Src to potentiate currents from NR2A/NR1 and NR2B/NR1 receptors expressed in Xenopus oocytes. The results show opposite effects of PSD‐95 coexpression on Src and insulin modulation of NR2A/NR1 receptor currents. Src potentiation of mouse NR2A/NR1 currents required PSD‐95 coexpression. In contrast, PSD‐95 coexpression eliminated insulin‐mediated potentiation of NR2A/NR1 receptor currents. PSD‐95 coexpression also eliminated PKC potentiation of NR2A/NR1 receptor currents. PSD‐95 may therefore play a key role in controlling kinase modulation of NR2A/NR1 receptor currents at glutamatergic synapses.