期刊
NEURON
卷 97, 期 5, 页码 1094-+出版社
CELL PRESS
DOI: 10.1016/j.neuron.2018.01.036
关键词
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资金
- AHA [11POST7020009, 14PRE19900021]
- Brain and Behavior Research Foundation NARSAD Young Investigator Grant [20748, T32 GM099608]
- NIH [R01 EY012347, R01 MH097887, R01 NS078792, R01 AG055357]
- NATIONAL EYE INSTITUTE [R01EY012347] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM099608] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF MENTAL HEALTH [R01MH097887] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R01NS078792] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE ON AGING [R01AG055357] Funding Source: NIH RePORTER
Despite the central role PSD-95 plays in anchoring postsynaptic AMPARs, how PSD-95 itself is tethered to postsynaptic sites is not well understood. Here we show that the F-actin binding protein alpha-actinin binds to the very N terminus of PSD-95. Knockdown (KD) of alpha-actinin phenocopies KD of PSD-95. Mutating lysine at position 10 or lysine at position 11 of PSD-95 to glutamate, or glutamate at position 53 or glutamate and aspartate at positions 213 and 217 of alpha-actinin, respectively, to lysine impairs, in parallel, PSD-95 binding to alpha-actinin and postsynaptic localization of PSD-95 and AMPARs. These experiments identify alpha-actinin as a critical PSD-95 anchor tethering the AMPAR-PSD-95 complex to postsynaptic sites.
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