Molecular dissociation of the role of PSD-95 in regulating synaptic strength and LTD.
作者： Weifeng Xu , Oliver M. Schlüter , Pascal Steiner , Brian L. Czervionke , Bernardo Sabatini
DOI: 10.1016/J.NEURON.2007.11.027
关键词:
摘要: The postsynaptic density protein PSD-95 influences synaptic AMPA receptor (AMPAR) content and may play a critical role in LTD. Here we demonstrate that the effects of on AMPAR-mediated responses LTD can be dissociated. Our findings suggest N-terminal-domain-mediated dimerization is important for PSD-95's effect basal AMPAR function, whereas C-terminal SH(3)-GK domains are also necessary localizing to synapses. We identify point mutants (Q15A, E17R) maintain influence yet block These increase proteolysis within its N-terminal domain, resulting fragment functions as dominant negative likely by scavenging signaling proteins required Thus, portion serves dual function. It localize at synapses scaffold
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