Regulation of AMPA receptor extrasynaptic insertion by 4.1N, phosphorylation and palmitoylation
Regulation of AMPA receptor extrasynaptic insertion by 4.1N, phosphorylation and palmitoylation
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New York: Nature Publishing Group US
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English
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New York: Nature Publishing Group US
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Contents
The authors use high-resolution total reflection fluorescence microscopy to study the mechanisms of AMPA receptor synaptic delivery. They report that palmitoylation of the GluR1 subunit modulates phosphorylation by PKC. This enhances protein 4.1N binding to GluR1, thereby facilitating GluR1 insertion.
The insertion of AMPA receptors (AMPARs) int...
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Full title
Regulation of AMPA receptor extrasynaptic insertion by 4.1N, phosphorylation and palmitoylation
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2712131
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2712131
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ISSN
1097-6256
E-ISSN
1546-1726
DOI
10.1038/nn.2351
