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RISS 인기검색어
- 검색키워드
- 저자 : Fitzjohn, Stephen M. (검색결과 2 건)
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LTP in hippocampal neurons is associated with a CaMKII‐mediated increase in GluA1 surface expression
Appleby, Vanessa J.,Corrê,a, Sonia A. L.,Duckworth, Joshua K.,Nash, Joanne E.,Noë,l, Jacques,Fitzjohn, Stephen M.,Collingridge, Graham L.,Molná,r, Elek Blackwell Publishing Ltd 2011 Journal of Neurochemistry Vol.116 No.4
<P> <I>J. Neurochem.</I> (2011) <B>116</B>, 530–543.</P><P><B>Abstract</B></P><P>The use of hippocampal dissociated neuronal cultures has enabled the study of molecular changes in endogenous native proteins associated with long‐term potentiation. Using immunofluorescence labelling of the active (Thr286‐phosphorylated) alpha‐Ca<SUP>2+</SUP>/calmodulin‐dependent protein kinase II (CaMKII) we found that CaMKII activity was increased by transient (3 × 1 s) depolarisation in 18‐ to 21‐day‐old cultures but not in 9‐ to 11‐day‐old cultures. The increase in Thr286 phosphorylation of CaMKII required the activation of NMDA receptors and was greatly attenuated by the CaMKII inhibitor KN‐62. We compared the effects of transient depolarisation on the surface expression of GluA1 and GluA2 subunits of the alpha‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazole propionate receptor and found a preferential recruitment of the GluA1 subunit. CaMKII inhibition prevented this NMDA receptor‐dependent delivery of GluA1 to the cell surface. CaMKII activation is therefore an important factor in the activity‐dependent recruitment of native GluA1 subunit‐containing alpha‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazole propionate receptors to the cell surface of hippocampal neurons.</P>
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Nash, Joanne E.,Appleby, Vanessa J.,Corrê,a, Sonia A. L.,Wu, Hongju,Fitzjohn, Stephen M.,Garner, Craig C.,Collingridge, Graham L.,Molná,r, Elek Blackwell Publishing Ltd 2010 Journal of Neurochemistry Vol.112 No.3
<P><I>J. Neurochem.</I> (2010) <B>112</B>, 677–690.</P><P>Abstract</P><P>Myosin VI is an actin-based motor protein that is enriched at the postsynaptic density and appears to interact with alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate-type glutamate receptors (AMPARs) via synapse associated protein 97 (SAP97). Here, we find that a Flag epitope-tagged dominant negative construct that inhibits the interaction between SAP97 and myosin VI (Flag-myoVI-DN) causes a dramatic reduction in the number of synapses and the surface expression of AMPARs in cultured hippocampal neurons. Furthermore, we find that Flag-myoVI-DN also prevents the rapid delivery of AMPARs to synapses that can be induced by the transient activation of <I>N</I>-methyl-<SMALL>D</SMALL>-aspartate receptors. The Flag-myoVI-DN induced decrease in surface AMPARs is not because of reduced AMPAR subunit protein synthesis. Using whole-cell recording, we show that Flag-myoVI-DN also prevents the activity-induced increase in miniature excitatory postsynaptic current frequency that is normally associated with recruitment of AMPARs to the cell surface at synaptic sites that lack these receptors (i.e. ‘silent’ synapses). Together, these results indicate that myosin VI/SAP97 plays an important role in trafficking and activity-dependent recruitment of AMPARs to synapses.</P>
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