GluA1 subunit ubiquitination mediates amyloid-β-induced loss of surface α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors
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The accumulation of soluble amyloid-β (Aβ) peptides produces profound neuronal changes in the brain during the pathogenesis of Alzheimer's disease. Excessive levels of Aβ disrupt excitatory synaptic transmission by promoting the removal of synaptic AMPA receptors (AMPARs), dendritic spine loss, and synaptic depression. Recently, activity-dependent ubiquitination of the GluA1 subunit has been shown to regulate the intracellular sorting of AMPARs toward late endosomes for degradation. However, whether this ubiquitin signaling pathway mediates Aβ-induced loss of surface AMPARs is unknown. In this study, we demonstrate that acute exposure of cultured neurons to soluble Aβ oligomers induces AMPAR ubiquitination concomitant with the removal of AMPARs from the plasma membrane. Importantly, expression of the GluA1 ubiquitin-deficient mutants inhibited the adverse effects of Aβ on the surface expression of AMPARs in neurons. Furthermore, we revealed the cross-talk between GluA1 ubiquitination and phosphorylation, in particular phosphorylation at Ser-845, which is crucial for AMPAR recycling and is known to be dephosphorylated in the presence of Aβ. Our data showed that the GluA1 ubiquitin-deficient mutant enhances GluA1 phosphorylation on Ser-845. Conversely, the GluA1 S845D phosphomimetic mutant reduced binding with Nedd4-1 and hence the ubiquitination of AMPARs. Importantly, the GluA1 S845D mutant also prevented Aβ-induced removal of surface AMPARs. Taken together, these findings provide the first demonstration of the dynamic cross-modulation of GluA1 ubiquitination and phosphorylation, a process that is perturbed by Aβ, in regulating the membrane sorting decision that ultimately determines the number of AMPARs on the cell surface.
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Ubiquitination and phosphorylation of GluA1 reciprocally inhibit each other, indicating complex cross talk of GluA1 PTMs may regulate LTP expression.
“Interestingly, ubiquination and phosphorylation of GluA1 reciprocally inhibit each other indicating that a complex cross talk of GluA1 PTMs may regulate LTP expression (Guntupalli et al., 2017).”
From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Guntupalli et al., 2017
The Results section, “The cross-talk between GluA1 phosphorylation and ubiquitination” (page unavailable), supports reciprocal inhibition at GluA1 Ser-845: ubiquitin-deficient mutants showed increased phosphorylation, while an S845D phosphomimetic showed reduced ubiquitination. The paper links this cross-talk to AMPA receptor trafficking and surface expression, but does not establish that it regulates LTP expression. (LLM, conf=0.85)
Experimental — accuracy not yet measuredPhosphorylated GluA1 S845 is resistant to ubiquitination.
“It has been shown that phosphorylated GluA1 S845 is resistant to ubiquitination (Guntupalli et al., 2017), offering a potential mechanism for the differential removal of phosphorylated and unphosphorylated GluA1 during scaling-down.”
From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Guntupalli et al., 2017
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Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420 · see citing works
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685 · see citing works
Reinsertion or Degradation of AMPA Receptors Determined by Activity-Dependent Endocytic Sorting
Ehlers, M. D. (2000) · Neuron · doi:10.1016/s0896-6273(00)00129-x · Cited by 1,096 · see citing works
Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation
Barria, A., Muller, D., Derkach, V., Griffith, L. C., & Soderling, T. R. (1997) · Science · doi:10.1126/science.276.5321.2042 · Cited by 1,049 · see citing works
AMPAR Removal Underlies Aβ-Induced Synaptic Depression and Dendritic Spine Loss
Hsieh, H., Boehm, J., Sato, C., Iwatsubo, T., Tomita, T., Sisodia, S., & Malinow, R. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.035 · Cited by 1,042 · see citing works
Neurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000 · see citing works
Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit
Roche, K. W., O'Brien, R. J., Mammen, A. L., Bernhardt, J., & Huganir, R. L. (1996) · Neuron · doi:10.1016/s0896-6273(00)80144-0 · Cited by 812 · see citing works
Self-citationRegulation of AMPA receptor trafficking and synaptic plasticity
Anggono, V., & Huganir, R. L. (2012) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2011.12.006 · Cited by 588 · see citing works
Self-citationMammen, A. L., Kameyama, K., Roche, K. W., & Huganir, R. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32528 · Cited by 441 · see citing works
Self-citationSynapses and Alzheimer's Disease
Sheng, M., Sabatini, B. L., & Sudhof, T. C. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005777 · Cited by 436 · see citing works
Beta-amyloid accumulation in APP mutant neurons reduces PSD-95 and GluR1 in synapses
Almeida, C. G., Tampellini, D., Takahashi, R. H., Greengard, P., Lin, M. T., Snyder, E. M., & Gouras, G. K. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.02.008 · Cited by 397 · see citing works
Barría, A., Derkach, V. A., & Soderling, T. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.32727 · Cited by 392 · see citing works
Man, H.-Y., Sekine-Aizawa, Y., & Huganir, R. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611698104 · Cited by 311 · see citing works
Self-citationRevett, T. J., Baker, G. B., Jhamandas, J. H., & Kar, S. (2012) · Journal of Psychiatry and Neuroscience · doi:10.1503/jpn.110190 · Cited by 294 · see citing works
Posttranslational regulation of AMPA receptor trafficking and function
Lü, W., & Roche, K. W. (2011) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2011.09.008 · Cited by 197 · see citing works
Long-term potentiation decay and memory loss are mediated by AMPAR endocytosis
Dong, Z., Han, H., Li, H., Bai, Y., Wang, W., Tu, M., Yan, P., Zhou, L., He, W., Wu, X., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci77888 · Cited by 194 · see citing works
Schwarz, L. A., Hall, B. J., & Patrick, G. N. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3686-10.2010 · Cited by 191 · see citing works
Stabilization of Ca 2+ -permeable AMPA receptors at perisynaptic sites by GluR1-S845 phosphorylation
He, K., Song, L., Cummings, L. W., Goldman, J. W., Huganir, R. L., & Lee, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910338106 · Cited by 189 · see citing works
Self-citationZhao, W.-Q., Santini, F., Breese, R., Ross, D., Zhang, X. D., Stone, D. J., Ferrer, M., Townsend, M., Wolfe, A. L., Seager, M. A., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.057182 · Cited by 188 · see citing works
Behavioral phenotypes of amyloid‐based genetically modified mouse models of Alzheimer's disease
Kobayashi, D. T., & Chen, K. S. (2005) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2005.00124.x · Cited by 175 · see citing works
Lussier, M. P., Sanz-Clemente, A., & Roche, K. W. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.652750 · Cited by 163 · see citing works
Nedd4‐mediated AMPA receptor ubiquitination regulates receptor turnover and trafficking
Lin, A. W., Hou, Q., Jarzylo, L. A., Amato, S., Gilbert, J. P., Shang, F., & Man, H. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07221.x · Cited by 158 · see citing works
Widagdo, J., Chai, Y. J., Ridder, M. C., Chau, Y. Q., Johnson, R. C., Sah, P., Huganir, R. L., & Anggono, V. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.01.015 · Cited by 132 · see citing works
Self-citationDewar, D., Chalmers, D. T., Graham, D. I., & McCulloch, J. (1991) · Brain Research · doi:10.1016/0006-8993(91)90230-s · Cited by 115 · see citing works
PICK1 loss of function occludes homeostatic synaptic scaling
Anggono, V., Clem, R. L., & Huganir, R. L. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.5633-10.2011 · Cited by 111 · see citing works
Self-citationAmyloid-<i>β</i>-Induced Dysregulation of AMPA Receptor Trafficking
Guntupalli, S., Widagdo, J., & Anggono, V. (2016) · Neural Plasticity · doi:10.1155/2016/3204519 · Cited by 110 · see citing works
Self-citationMiñano-Molina, A. J., España, J., Martín, E., Barneda‐Zahonero, B., Fadó, R., Solé, M., Trullás, R., Saura, C. A., & Rodrı́guez-Álvarez, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.227504 · Cited by 103 · see citing works
Roles of stargazin and phosphorylation in the control of AMPA receptor subcellular distribution
Kessels, H. W. H. G., Kopec, C. D., Klein, M. E., & Malinow, R. (2009) · Nature Neuroscience · doi:10.1038/nn.2340 · Cited by 96 · see citing works
Extensive phosphorylation of AMPA receptors in neurons
Diering, G. H., Heo, S., Hussain, N. K., Liu, B., & Huganir, R. L. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610631113 · Cited by 90 · see citing works
Self-citationLiu, S.-J., Gasperini, R., Foa, L., & Small, D. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-091654 · Cited by 84 · see citing works
Anggono, V., Koç-Schmitz, Y., Widagdo, J., Kormann, J., Quan, A., Chen, C.-M., Robinson, P., Choi, S.-Y., Linden, D. J., Plomann, M., et al. (2013) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1312467110 · Cited by 81 · see citing works
Self-citationYasuda, R. P., Ikonomović, M. D., Sheffield, R., Rubín, R. T., Wolfe, B. B., & Armstrong, D. M. (1995) · Brain Research · doi:10.1016/0006-8993(95)00178-s · Cited by 80 · see citing works
Aβ-Induced Synaptic Alterations Require the E3 Ubiquitin Ligase Nedd4-1
Rodrigues, E. M., Scudder, S. L., Goo, M. S., & Patrick, G. N. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2964-15.2016 · Cited by 67 · see citing works
Synapto‐depressive effects of amyloid beta require PICK 1
Alfonso, S., Kessels, H. W. H. G., Banos, C. C., Chan, T. R., Lin, E. Y.-S., Kumaravel, G., Scannevin, R. H., Rhodes, K. J., Huganir, R. L., Guckian, K. M., et al. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12499 · Cited by 62 · see citing works
Self-citationUbiquitin-dependent trafficking and turnover of ionotropic glutamate receptors
Goo, M. S., Scudder, S. L., & Patrick, G. N. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00060 · Cited by 49 · see citing works
PACSIN1 regulates the dynamics of AMPA receptor trafficking
Widagdo, J., Fang, H., Jang, S., & Anggono, V. (2016) · Scientific Reports · doi:10.1038/srep31070 · Cited by 49 · see citing works
Self-citationUbiquitin signals the demise of AMPA receptors
Widagdo, J., & Anggono, V. (2015) · Oncotarget · doi:10.18632/oncotarget.4645 · Cited by 4 · see citing works
Self-citation
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- [33]Alfonso S., Kessels H. W., Banos C. C., Chan T. R., Lin E. T., Kumaravel G., Scannevin R. H., Rhodes K. J., Huganir R., Guckian K. M., Dunah A. W., and Malinow R. (2014) Synapto-depressive effects of amyloid β require PICK1. Eur. J. Neurosci. 39, 1225– 1233 24713001 PMC3983572
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Self-citationLópez, J. A., González, H. M., & Léger, G. C. (2019) · Handbook of clinical neurology · doi:10.1016/b978-0-12-804766-8.00013-3 · Cited by 834 · see citing works
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Styr, B., & Slutsky, I. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0080-x · Cited by 314 · see citing works
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Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.11.006 · Cited by 258 · see citing works
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Babaei, P. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174310 · Cited by 149 · see citing works
Lee, A., Kondapalli, C., Virga, D. M., Lewis, T. L., Koo, S. Y., Ashok, A., Mairet‐Coello, G., Herzig, S., Foretz, M., Viollet, B., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32130-5 · Cited by 113 · see citing works
Ferguson, S. M. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.04.005 · Cited by 101 · see citing works
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Mroczko, B., Groblewska, M., Litman-Zawadzka, A., Kornhuber, J., & Lewczuk, P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19071884 · Cited by 97 · see citing works
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Sciaccaluga, M., Megaro, A., Bellomo, G., Ruffolo, G., Romoli, M., Palma, E., & Costa, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115991 · Cited by 70 · see citing works
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Self-citationQu, W., Yuan, B., Li, R., Liu, Q., Zhang, X., Cui, R., Yang, W., & Li, B. (2020) · Cell Proliferation · doi:10.1111/cpr.12959 · Cited by 64 · see citing works
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Tehran, D. A., Kochlamazashvili, G., Pampaloni, N. P., Sposini, S., Shergill, J. K., Lehmann, M., Pashkova, N., Schmidt, C., Löwe, D., Napieczyńska, H., et al. (2022) · Science Advances · doi:10.1126/sciadv.abl5032 · Cited by 29 · see citing works
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Guntupalli, S., Park, P., Han, D. H., Zhang, L., Yong, X. L. H., Ringuet, M. T., Blackmore, D. G., Jhaveri, D. J., Köentgen, F., Widagdo, J., et al. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.1542-22.2023 · Cited by 25 · see citing works
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Gu, X., Wu, H., Xie, Y., Xu, L., Liu, X., & Wang, W. (2021) · Molecular Medicine · doi:10.1186/s10020-021-00273-8 · Cited by 21 · see citing works
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Долгачева, Л. П., Tuleukhanov, S. T., & Зинченко, В. П. (2020) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747820030046 · Cited by 7 · see citing works
Nong, Y., Kim, J. S., Jia, L., Arancio, O., & Wang, Q. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251342273 · Cited by 7 · see citing works
Subunit-Specific Augmentation of AMPA Receptor Ubiquitination by Phorbol Ester
Widagdo, J., Kerk, J. W., Guntupalli, S., Huganir, R., & Anggono, V. (2020) · Cellular and molecular neurobiology · doi:10.1007/s10571-020-00809-2 · Cited by 6 · see citing works
Self-citationSingle cell molecular alterations reveal target cells and pathways of conditioned fear memory
Shen, M., Shang, M., Tian, R.-F., Hu, Y., Han, Q., Hu, J., An, G., Wang, B., Cao, Z., Lin, X., et al. (2023) · Brain Research · doi:10.1016/j.brainres.2023.148309 · Cited by 7 · see citing works
Midorikawa, R., Wakazono, Y., & Takamiya, K. (2024) · Journal of Cell Science · doi:10.1242/jcs.261281 · Cited by 6 · see citing works
Yao, H., Guo, W., Suo, L.-L., Li, G., Wang, Y.-S., Chen, Y., Sun, Y., & Ding, R. (2022) · Behavioural Brain Research · doi:10.1016/j.bbr.2022.113813 · Cited by 6 · see citing works
Jaye, S., Sandau, U. S., McFarland, T. J., Woltjer, R. L., & Saugstad, J. A. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1426180 · Cited by 5 · see citing works
Min-Kaung-Wint-Mon, & Mitsushima, D. (2025) · Journal of dementia and Alzheimer's disease · doi:10.3390/jdad2030025 · Cited by 5 · see citing works
Hodul, M., Rennich, B. J., Luth, E. S., Dahlberg, C. L., & Juo, P. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.1074-20.2021 · Cited by 5 · see citing works
Suri, K., Ramesh, M., Bhandari, M., Gupta, V., Kumar, V., Govindaraju, T., & Murugan, N. A. (2024) · ChemBioChem · doi:10.1002/cbic.202400224 · Cited by 5 · see citing works
Redondo, J., Popik, B., Casagrande, M. A., Silva, M. O., Quillfeldt, J. A., Alvares, L. D. O., & Souza, T. M. E. (2019) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2019.107135 · Cited by 5 · see citing works
Ubiquitination in ischemic stroke: Molecular mechanisms and therapeutic implications
Zhang, K., Ruan, X., Chen, Z., Wang, S., Hu, B., Wen, Z., & Wang, H. (2026) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2026.112028 · Cited by 3 · see citing works
Unraveling Molecular and System Processes for Fear Memory
Souza, T. M. E. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.03.015 · Cited by 3 · see citing works
The mevalonate suppressor δ-tocotrienol increases AMPA receptor-mediated neurotransmission
Wei, W., Yount, S. T., Allen, Z. D., Bechdol, K., Xia, W., Mo, H., & Mabb, A. M. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.11.052 · Cited by 3 · see citing works
Chen, P., Yao, C., Chien, P., Tsai, H.-J., Chen, Y., Chuang, J.-H., Chou, P.-L., Lee, G.-C., Lin, W., & Lin, Y. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00633 · Cited by 3 · see citing works
Koppin, A., & Chase, L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910271 · Cited by 3 · see citing works
Hiskens, M. I. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.2018-23.2024 · Cited by 2 · see citing works
Li, Y., Hou, X., & Tao, Y. (2026) · Neuroscience · doi:10.1016/j.neuroscience.2026.04.025
Posttranslational modifications of AMPA receptors in synaptic function and memory
de León-López, C. A. M., Navarro‐Lobato, I., & Khan, Z. U. (2026) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-026-06297-9
Distinct roles of AMPA receptor subunits as potential therapeutic targets in Alzheimer’s disease
Seo, J., Kim, K., & Park, M. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2026.108394
Joshi, A., Salunkhe, J., & Ugale, V. G. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12722-w
NEDD4-1: from molecular mechanisms to clinical translation in human diseases
Tian, H., Huang, Y., Liang, Y., Huang, C., Wei, B., Liao, C.-N., & Zhou, W. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1897001
- Authors
- Guntupalli, S., Jang, S. E., Zhu, T., Huganir, R. L., Widagdo, J., & Anggono, V.
- Affiliations
- The University of Queensland (AU)
- Johns Hopkins University (US)
- Corresponding author
- Anggono, Victor
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2017-05
- Volume
- 292
- Issue
- 20
- Pages
- 8186-8194
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC5437227
- OpenAlex
- W2604570082
- Cited by
- 70
- References
- 40
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 10 · 2023: 8 · 2022: 9 · 2021: 9 · 2020: 6 · 2019: 7 · 2018: 7 · 2017: 3
- FWCI
- 3.08
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- John T. Reid Charitable Trusts
- Alzheimer's Australia Dementia Research Foundation (DGP14–57)
- National Health and Medical Research Council (GNT1083209, GNT1099114, 477108)
- Australian Research Council (DE170100112)
- University of Queensland
- National Institutes of Health (P50AG005146)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- GluR1, AMPA receptors, amyloid-beta, ubiquitination, phosphorylation, NEDD4-1, receptor internalization, synaptic plasticity, Alzheimer's disease, membrane sorting, excitatory synaptic transmission, phosphomimetic mutant
- MeSH terms
- Nedd4 Ubiquitin Protein Ligases, Animals, Cells, Cultured, Neurons, Peptide Fragments, Phosphorylation, Amyloid beta-Peptides, Receptors, AMPA, Amino Acid Substitution, Mutation, Missense, Ubiquitin-Protein Ligases, Rats, Ubiquitination, Endosomal Sorting Complexes Required for Transport
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