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Sorting Nexin 27 regulates basal and activity-dependent trafficking of AMPARs.

Authors: Hussain, Natasha K  Diering, Graham H  Sole, Jonathan  Anggono, Victor  Huganir, Richard L 
Citation: Hussain NK, etal., Proc Natl Acad Sci U S A. 2014 Aug 12;111(32):11840-5. doi: 10.1073/pnas.1412415111. Epub 2014 Jul 28.
Pubmed: (View Article at PubMed) PMID:25071192
DOI: Full-text: DOI:10.1073/pnas.1412415111

Activity-dependent changes in synaptic strength have long been postulated as cellular correlates of learning and memory. Long-term potentiation (LTP), a well characterized form of synaptic plasticity, is often expressed as an increase in the number of postsynaptic AMPA-type glutamate receptors (AMPARs). Although the precise molecular mechanisms governing LTP remain elusive, this study identifies one member of the sorting nexin family, Sorting Nexin 27 (SNX27), as a critical component in this process. The ability of sorting nexins to bind specific phospholipids as well as their propensity to form protein-protein complexes, points to a role for these proteins in membrane trafficking and protein sorting. Here, we demonstrate that SNX27 binds to AMPARs, and that this interaction is regulated in an activity-dependent manner. Furthermore, we provide evidence that SNX27 is synaptically enriched and its level of expression regulates targeting of AMPARs to the neuronal surface. Loss of SNX27 abolishes recruitment of surface AMPARs during chemical LTP. Collectively, our data suggest a role for SNX27 in modulating synaptic plasticity through regulated interaction with AMPARs.

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CRRD Object Information
CRRD ID: 13508620
Created: 2018-03-05
Species: All species
Last Modified: 2018-03-05
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.