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Park, Pojeong,Sanderson, Thomas M.,Amici, Mascia,Choi, Sun-Lim,Bortolotto, Zuner A.,Zhuo, Min,Kaang, Bong-Kiun,Collingridge, Graham L. Society for Neuroscience 2016 The Journal of neuroscience Vol.36 No.2
<P>Two forms of NM DA receptor (NMDAR)-dependent long-term potentiation (LIP) at hippocampal CAI synapses can be distinguished based on their sensitivity to inhibitors of protein kinase A (PKA). The PKA-dependent form requires multiple episodes of high-frequency stimulation (HFS) or theta burst stimuli (TBS) with a spacing between episodes in the order of minutes. To investigate the mechanism by which spaced episodes induce the PKA-dependent form of LIP, we have compared, in interleaved experiments, spaced (s) and compressed (c) TBS protocols in the rat CAI synapses. We find that LIP induced by sTBS, but not that induced by cTBS, involves the insertion of calcium-permeable (CP) AMPARs, as assessed using pharmacological and electrophysiological criteria. Furthermore, a single TBS when paired with rolipram [4-(3-(cyclopentyloxy)-4-methoxyphenyl)pyrrolidin-2-one], to activate PKA, generates an LTP that also involves the insertion of CP-AMPARs. These data demonstrate that the involvement of CP-AMPARs in LTP is critically determined by the timing of the induction trigger and is associated specifically with the PKA-dependent form of LIP.</P>
The JAK/STAT Pathway Is Involved in Synaptic Plasticity
Nicolas, Cé,line ,S.,Peineau, Sté,phane,Amici, Mascia,Csaba, Zsolt,Fafouri, Assia,Javalet, Charlotte,Collett, Valerie ,J.,Hildebrandt, Lars,Seaton, Gillian,Choi, Sun-Lim,Sim, Su-Eo Cell Press 2012 Neuron Vol.73 No.2
<▼1><P><B>Summary</B></P><P>The Janus kinase (JAK)/signal transducer and activator of transcription (STAT) pathway is involved in many cellular processes, including cell growth and differentiation, immune functions and cancer. It is activated by various cytokines, growth factors, and protein tyrosine kinases (PTKs) and regulates the transcription of many genes. Of the four JAK isoforms and seven STAT isoforms known, JAK2 and STAT3 are highly expressed in the brain where they are present in the postsynaptic density (PSD). Here, we demonstrate a new neuronal function for the JAK/STAT pathway. Using a variety of complementary approaches, we show that the JAK/STAT pathway plays an essential role in the induction of NMDA-receptor dependent long-term depression (NMDAR-LTD) in the hippocampus. Therefore, in addition to established roles in cytokine signaling, the JAK/STAT pathway is involved in synaptic plasticity in the brain.</P></▼1><▼2><P>The authors demonstrate a new neuronal function for the JAK/STAT pathway in the induction of NMDA-receptor-dependent long-term depression (NMDAR-LTD) in the hippocampus.</P></▼2>
Muscarinic receptors induce LTD of NMDAR EPSCs via a mechanism involving hippocalcin, AP2 and PSD-95
Jo, Jihoon,Son, Gi Hoon,Winters, Bryony L,Kim, Myung Jong,Whitcomb, Daniel J,Dickinson, Bryony A,Lee, Youn-Bok,Futai, Kensuke,Amici, Mascia,Sheng, Morgan,Collingridge, Graham L,Cho, Kwangwook Nature Publishing Group, a division of Macmillan P 2010 NATURE NEUROSCIENCE Vol.13 No.10
Although muscarinic acetylcholine receptors (mAChRs) and NMDA receptors (NMDARs) are important for synaptic plasticity, learning and memory, the manner in which they interact is poorly understood. We found that stimulation of muscarinic receptors, either by an agonist or by the synaptic release of acetylcholine, led to long-term depression (LTD) of NMDAR-mediated synaptic transmission. This form of LTD involved the release of Ca<SUP>2+</SUP> from IP<SUB>3</SUB>-sensitive intracellular stores and was expressed via the internalization of NMDARs. Our results suggest that the molecular mechanism involves a dynamic interaction between the neuronal calcium sensor protein hippocalcin, the clathrin adaptor molecule AP2, the postsynaptic density enriched protein PSD-95 and NMDARs. We propose that hippocalcin binds to the SH3 region of PSD-95 under basal conditions, but it translocates to the plasma membrane on sensing Ca<SUP>2+</SUP>; in doing so, it causes PSD-95 to dissociate from NMDARs, permitting AP2 to bind and initiate their dynamin-dependent endocytosis.