Proteomic Analysis of α-Amino-3-hydroxy-5-methyl-4-isoxazole Propionate Receptor Complexes
Open accessAbstract
The AMPA receptor (AMPA-R) is a major excitatory neurotransmitter receptor in the brain. Identifying and characterizing the neuronal proteins interacting with AMPA-Rs have provided important information about the molecular mechanisms underlying synaptic transmission and plasticity. In this study, to identify more AMPA-R interactors in vivo, we performed proteomic analyses of AMPA-R complexes from the brain. AMPA-R complexes were isolated from the brain through various combinations of biochemical techniques for solubilization, enrichment, and immunoprecipitation. Mass spectrometry analyses of these isolated complexes identified several novel components of the AMPA-R complexes as well as some previously identified components. The identification of these novel components helps to further define the complex mechanisms involved in the regulation of AMPA receptor function and synaptic plasticity.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
DOCK9 interacts with neural AMPA receptors.
“Proteomic analysis indicated that DOCK9 interacts with neural AMPA receptors, which regulate synaptic plasticity (124).”
From RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors (2021) · cites this paper as [124]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Emotion Enhances Learning via Norepinephrine Regulation of AMPA-Receptor Trafficking
Hu, H., Real, E., Takamiya, K., Kang, M.-G., Ledoux, J., Huganir, R. L., & Malinow, R. (2007) · Cell · doi:10.1016/j.cell.2007.09.017 · Cited by 496 · see citing works
Self-citationSteinberg, J. P., Takamiya, K., Shen, Y., Xia, J., Rubio, M. E., Yu, S., Jin, W., Thomas, G. M., Linden, D. J., & Huganir, R. L. (2006) · Neuron · doi:10.1016/j.neuron.2006.02.025 · Cited by 288 · see citing works
Self-citationXu, D., Hopf, C., Reddy, R., Cho, R. W., Guo, L., Lanahan, A., Petralia, R. S., Wenthold, R. J., O'Brien, R. J., & Worley, P. (2003) · Neuron · doi:10.1016/s0896-6273(03)00463-x · Cited by 265 · see citing works
Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins
Meller, N., Irani-Tehrani, M., Kiosses, W. B., Del Pozo, M. A., & Schwartz, M. A. (2002) · Nature Cell Biology · doi:10.1038/ncb835 · Cited by 171 · see citing works
Kang, M.-G., Guo, Y., & Huganir, R. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812861106 · Cited by 82 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 42
- [1]Hsieh H. Boehm J. Sato C. Iwatsubo T. Tomita T. Sisodia S. Malinow R. (2006) AMPAR removal underlies Aβ-induced synaptic depression and dendritic spine loss. Neuron 52, 831– 843 17145504 PMC1850952
- [2]Koh S. Tibayan F. D. Simpson J. N. Jensen F. E. (2004) NBQX or topiramate treatment after perinatal hypoxia-induced seizures prevents later increases in seizure-induced neuronal injury. Epilepsia 45, 569– 575 15144420
- [3]Li B. Woo R. S. Mei L. Malinow R. (2007) The neuregulin-1 receptor erbB4 controls glutamatergic synapse maturation and plasticity. Neuron 54, 583– 597 17521571 PMC2031848
- [4]Pilpel Y. Kolleker A. Berberich S. Ginger M. Frick A. Mientjes E. Oostra B. A. Seeburg P. H. (2009) Synaptic ionotropic glutamate receptors and plasticity are developmentally altered in the CA1 field of Fmr1 knockout mice. J. Physiol. 587, 787– 804 19103683 PMC2669971
- [5]Dong H. O'Brien R. J. Fung E. T. Lanahan A. A. Worley P. F. Huganir R. L. (1997) GRIP. A synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature 386, 279– 284 9069286
- [6]Nishimune A. Isaac J. T. Molnar E. Noel J. Nash S. R. Tagaya M. Collingridge G. L. Nakanishi S. Henley J. M. (1998) NSF binding to GluR2 regulates synaptic transmission. Neuron 21, 87– 97 9697854
- [7]Osten P. Srivastava S. Inman G. J. Vilim F. S. Khatri L. Lee L. M. States B. A. Einheber S. Milner T. A. Hanson P. I. Ziff E. B. (1998) The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and α-and β-SNAPs. Neuron 21, 99– 110 9697855
- [8]Shen L. Liang F. Walensky L. D. Huganir R. L. (2000) Regulation of AMPA receptor GluR1 subunit surface expression by a 4.1N-linked actin cytoskeletal association. J. Neurosci. 20, 7932– 7940 11050113 PMC6772741
- [9]Song I. Kamboj S. Xia J. Dong H. Liao D. Huganir R. L. (1998) Interaction of the N-ethylmaleimide-sensitive factor with AMPA receptors. Neuron 21, 393– 400 9728920
- [10]Xia J. Zhang X. Staudinger J. Huganir R. L. (1999) Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1. Neuron 22, 179– 187 10027300
- [11]Boehm J. Kang M. G. Johnson R. C. Esteban J. Huganir R. L. Malinow R. (2006) Synaptic incorporation of AMPA receptors during LTP is controlled by a PKC phosphorylation site on GluR1. Neuron 51, 213– 225 16846856
- [12]Chung H. J. Steinberg J. P. Huganir R. L. Linden D. J. (2003) Requirement of AMPA receptor GluR2 phosphorylation for cerebellar long term depression. Science 300, 1751– 1755 12805550
- [13]Lee H. K. Barbarosie M. Kameyama K. Bear M. F. Huganir R. L. (2000) Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity. Nature 405, 955– 959 10879537
- [14]Lee H. K. Kameyama K. Huganir R. L. Bear M. F. (1998) NMDA induces long term synaptic depression and dephosphorylation of the GluR1 subunit of AMPA receptors in hippocampus. Neuron 21, 1151– 1162 9856470
- [17]Lee H. K. Takamiya K. Han J. S. Man H. Kim C. H. Rumbaugh G. Yu S. Ding L. He C. Petralia R. S. Wenthold R. J. Gallagher M. Huganir R. L. (2003) Phosphorylation of the AMPA receptor GluR1 subunit is required for synaptic plasticity and retention of spatial memory. Cell 112, 631– 643 12628184
- [18]Lin D. T. Makino Y. Sharma K. Hayashi T. Neve R. Takamiya K. Huganir R. L. (2009) Regulation of AMPA receptor extrasynaptic insertion by 4.1N, phosphorylation, and palmitoylation. Nat. Neurosci. 12, 879– 887 19503082 PMC2712131
- [19]Hayashi T. Rumbaugh G. Huganir R. L. (2005) Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites. Neuron 47, 709– 723 16129400
- [20]Husi H. Ward M. A. Choudhary J. S. Blackstock W. P. Grant S. G. (2000) Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. Nat. Neurosci. 3, 661– 669 10862698
- [21]Peng J. Kim M. J. Cheng D. Duong D. M. Gygi S. P. Sheng M. (2004) Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry. J. Biol. Chem. 279, 21003– 21011 15020595
- [22]Müller C. S. Haupt A. Bildl W. Schindler J. Knaus H. G. Meissner M. Rammner B. Striessnig J. Flockerzi V. Fakler B. Schulte U. (2010) Quantitative proteomics of the Cav2 channel nano-environments in the mammalian brain. Proc. Natl. Acad. Sci. U.S.A. 107, 14950– 14957 20668236 PMC2930569
- [23]Kang M. G. Chen C. C. Felix R. Letts V. A. Frankel W. N. Mori Y. Campbell K. P. (2001) Biochemical and biophysical evidence for γ2 subunit association with neuronal voltage-activated Ca2+ channels. J. Biol. Chem. 276, 32917– 32924 11441000
- [24]Guo Y. Ma S. F. Grigoryev D. Van Eyk J. Garcia J. G. (2005) 1-DE MS and 2-D LC-MS analysis of the mouse bronchoalveolar lavage proteome. Proteomics 5, 4608– 4624 16240291
- [25]Kanagawa M. Saito F. Kunz S. Yoshida-Moriguchi T. Barresi R. Kobayashi Y. M. Muschler J. Dumanski J. P. Michele D. E. Oldstone M. B. Campbell K. P. (2004) Molecular recognition by LARGE is essential for expression of functional dystroglycan. Cell 117, 953– 964 15210115
- [26]Wang Y. Liu X. Biederer T. Südhof T. C. (2002) A family of RIM-binding proteins regulated by alternative splicing. Implications for the genesis of synaptic active zones. Proc. Natl. Acad. Sci. U.S.A. 99, 14464– 14469 12391317 PMC137906
- [27]Kang M. G. Chen C. C. Wakamori M. Hara Y. Mori Y. Campbell K. P. (2006) A functional AMPA receptor-calcium channel complex in the postsynaptic membrane. Proc. Natl. Acad. Sci. U.S.A. 103, 5561– 5566 16567654 PMC1459393
- [29]Blackstone C. D. Moss S. J. Martin L. J. Levey A. I. Price D. L. Huganir R. L. (1992) Biochemical characterization and localization of a non-N-methyl-d-aspartate glutamate receptor in rat brain. J. Neurochem. 58, 1118– 1126 1371146
- [30]Martin L. J. Blackstone C. D. Levey A. I. Huganir R. L. Price D. L. (1993) AMPA glutamate receptor subunits are differentially distributed in rat brain. Neuroscience 53, 327– 358 8388083
- [33]Chang Y. C. Wu T. Y. Li B. F. Gao L. H. Liu C. I. Wu C. L. (1996) Purification and biochemical characterization of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid/kainate-sensitive l-glutamate receptors of pig brain. Biochem. J. 319, 49– 57 8870648 PMC1217734
- [34]Clark R. A. Gurd J. W. Bissoon N. Tricaud N. Molnar E. Zamze S. E. Dwek R. A. McIlhinney R. A. Wing D. R. (1998) Identification of lectin-purified neural glycoproteins, GPs 180, 116, and 110, with NMDA and AMPA receptor subunits. Conservation of glycosylation at the synapse. J. Neurochem. 70, 2594– 2605 9603226
- [35]Wenthold R. J. Petralia R. S. Blahos J. II Niedzielski A. S. (1996) Evidence for multiple AMPA receptor complexes in hippocampal CA1/CA2 neurons. J. Neurosci. 16, 1982– 1989 8604042 PMC6578515
- [36]Yan Z. Hsieh-Wilson L. Feng J. Tomizawa K. Allen P. B. Fienberg A. A. Nairn A. C. Greengard P. (1999) Protein phosphatase 1 modulation of neostriatal AMPA channels. Regulation by DARPP-32 and spinophilin. Nat. Neurosci. 2, 13– 17 10195174
- [37]Rubio M. E. Wenthold R. J. (1999) Calnexin and the immunoglobulin binding protein (BiP) coimmunoprecipitate with AMPA receptors. J. Neurochem. 73, 942– 948 10461883
- [38]Moon I. S. Park I. S. Schenker L. T. Kennedy M. B. Moon J. I. Jin I. (2001) Presence of both constitutive and inducible forms of heat shock protein 70 in the cerebral cortex and hippocampal synapses. Cereb. Cortex 11, 238– 248 11230095
- [39]Kuramoto K. Negishi M. Katoh H. (2009) Regulation of dendrite growth by the Cdc42 activator Zizimin1/Dock9 in hippocampal neurons. J. Neurosci. Res. 87, 1794– 1805 19156867
- [40]Wiens K. M. Lin H. Liao D. (2005) Rac1 induces the clustering of AMPA receptors during spinogenesis. J. Neurosci. 25, 10627– 10636 16291935 PMC6725855
- [41]Shepherd J. D. Huganir R. L. (2007) The cell biology of synaptic plasticity. AMPA receptor trafficking. Annu. Rev. Cell Dev. Biol. 23, 613– 643 17506699
- [42]Cingolani L. A. Goda Y. (2008) Actin in action. the interplay between the actin cytoskeleton and synaptic efficacy. Nat. Rev. Neurosci. 9, 344– 356 18425089
- [43]Ohtsuka T. Takao-Rikitsu E. Inoue E. Inoue M. Takeuchi M. Matsubara K. Deguchi-Tawarada M. Satoh K. Morimoto K. Nakanishi H. Takai Y. (2002) Cast. A novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and munc13–1. J. Cell Biol. 158, 577– 590 12163476 PMC2173811
- [44]Sia G. M. Béïque J. C. Rumbaugh G. Cho R. Worley P. F. Huganir R. L. (2007) Interaction of the N-terminal domain of the AMPA receptor GluR4 subunit with the neuronal pentraxin NP1 mediates GluR4 synaptic recruitment. Neuron 55, 87– 102 17610819
- [45]Mikiewicz K. Jose L. E. Bento-Abreu A. Fislage M. Taes I. Kasprowicz J. Swerts J. Sigrist S. Versées W. Robberecht W. Verstreken P. (2011) ELP3 controls active zone morphology by acetylating the ELKS family member Bruchpilot. Neuron 72, 776– 788 22153374
- [46]Hida Y. Ohtsuka T. (2010) CAST and ELKS proteins. Structural and functional determinants of the presynaptic active zone. J. Biochem. 148, 131– 137 20581014
- [47]Fanning A. S. Anderson J. M. (2009) Zonula occludens-1 and -2 are cytosolic scaffolds that regulate the assembly of cellular junctions. Ann. N.Y. Acad. Sci. 1165, 113– 120 19538295 PMC3759978
Cited by
Sorted by citations
Thompson, A. P., Bitsina, C., Gray, J. L., von Delft, F., & Brennan, P. E. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100521 · Cited by 21 · see citing works
- Authors
- Kang, M.-G., Nuriya, M., Guo, Y., Martindale, K. D., Lee, D. Z., & Huganir, R. L.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of California San Diego (US)
- The University of Texas Medical Branch at Galveston (US)
- Corresponding author
- Kang, Myoung-Goo
- Huganir, Richard L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-08
- Volume
- 287
- Issue
- 34
- Pages
- 28632-28645
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3436506
- OpenAlex
- W1963726213
- Cited by
- 29
- References
- 5
- Citations by year
- 2025: 1 · 2024: 1 · 2022: 1 · 2021: 3 · 2020: 4 · 2018: 3 · 2017: 5 · 2016: 1 · 2015: 4 · 2014: 4 · 2013: 2
- FWCI
- 1.32
- 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-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health (n01hv28180-13-0-0)
- National Heart, Lung, and Blood Institute (N01 HV-28180, N01 HV028180)
- National Institute of Neurological Disorders and Stroke (R01NS036715)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- AMPA receptors, receptor complex, protein interactors, synaptic plasticity, brain, receptor regulation, synaptic transmission
- MeSH terms
- Animals, Synaptic Transmission, Receptors, AMPA, Proteomics, Multiprotein Complexes, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review