Splice variants of the glutamate transporter GLT1 form hetero-oligomers that interact with PSD-95 and NMDA receptors
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چکیده
منابع مشابه
Cellular/Molecular PSD-95 Uncouples Dopamine–Glutamate Interaction in the D1/PSD-95/NMDA Receptor Complex
Jingping Zhang,1 Tai-Xiang Xu,1 Penelope J. Hallett,2 Masahiko Watanabe,3 Seth G. N. Grant,4 Ole Isacson,2 and Wei-Dong Yao1 1New England Primate Research Center, Harvard Medical School, Southborough, Massachusetts 01772, 2McLean Hospital, Harvard Medical School, Belmont, Massachusetts 02478, 3Department of Anatomy, Hokkaido University School of Medicine, Sapporo 060-8638, Japan, and 4Wellcome ...
متن کاملPSD-95 uncouples dopamine-glutamate interaction in the D1/PSD-95/NMDA receptor complex.
Classical dopaminergic signaling paradigms and emerging studies on direct physical interactions between the D(1) dopamine (DA) receptor and the NMDA glutamate receptor predict a reciprocally facilitating, positive feedback loop. This loop, if not controlled, may cause concomitant overactivation of both D(1) and NMDA receptors, triggering neurotoxicity. Endogenous protective mechanisms must exis...
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Lipin family members (lipin 1, 2 and 3) are bi-functional proteins that dephosphorylate PA (phosphatidic acid) to produce DAG (diacylglycerol) and act in the nucleus to regulate gene expression. Although other components of the triacylglycerol synthesis pathway can form oligomeric complexes, it is unknown whether lipin proteins also exist as oligomers. In the present study, using various approa...
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The development of glutamatergic synapses involves changes in the number and type of receptors present at the postsynaptic density. To elucidate molecular mechanisms underlying these changes, we combine in utero electroporation of constructs that alter the molecular composition of developing synapses with dual whole-cell electrophysiology to examine synaptic transmission during two distinct dev...
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NMDA receptor (NMDAR) composition and synaptic retention represent pivotal features in the physiology and pathology of excitatory synapses. Here, we identify Rabphilin 3A (Rph3A) as a new GluN2A subunit-binding partner. Rph3A is known as a synaptic vesicle-associated protein involved in the regulation of exo- and endocytosis processes at presynaptic sites. We find that Rph3A is enriched at dend...
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ژورنال
عنوان ژورنال: Journal of Neurochemistry
سال: 2009
ISSN: 0022-3042,1471-4159
DOI: 10.1111/j.1471-4159.2009.06125.x