Local palmitoylation cycles define activity-regulated postsynaptic subdomains
Open accessAbstract
Distinct PSD-95 clusters are primary landmarks of postsynaptic densities (PSDs), which are specialized membrane regions for synapses. However, the mechanism that defines the locations of PSD-95 clusters and whether or how they are reorganized inside individual dendritic spines remains controversial. Because palmitoylation regulates PSD-95 membrane targeting, we combined a conformation-specific recombinant antibody against palmitoylated PSD-95 with live-cell super-resolution imaging and discovered subsynaptic nanodomains composed of palmitoylated PSD-95 that serve as elementary units of the PSD. PSD-95 in nanodomains underwent continuous de/repalmitoylation cycles driven by local palmitoylating activity, ensuring the maintenance of compartmentalized PSD-95 clusters within individual spines. Plasma membrane targeting of DHHC2 palmitoyltransferase rapidly recruited PSD-95 to the plasma membrane and proved essential for postsynaptic nanodomain formation. Furthermore, changes in synaptic activity rapidly reorganized PSD-95 nano-architecture through plasma membrane-inserted DHHC2. Thus, the first genetically encoded antibody sensitive to palmitoylation reveals an instructive role of local palmitoylation machinery in creating activity-responsive PSD-95 nanodomains, contributing to the PSD (re)organization.
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?
The average estimated diameter of RIM1/2 nanoclusters is very close to the reported size of PSD-95 and AMPA receptor nanoclusters.
“The average estimated diameter of ~80 nm for RIM1/2 NCs was very close to the reported size of PSD-95 and AMPA receptor (AMPAR) NCs4–6.”
From A trans-synaptic nanocolumn aligns neurotransmitter release to receptors (2016) · cites this paper as [6]
The Results section (page unavailable) reports a mean diameter of about 200 nm for palmitoylated PSD-95 nanodomains, not a size very close to the citing sentence’s ~80 nm. It reports that AMPAR clusters associate with those nanodomains but gives no AMPAR-cluster diameter. (LLM, conf=0.86)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredPresynaptic RIM nanoclusters closely align with concentrated postsynaptic receptors and scaffolding proteins.
“These presynaptic RIM nanoclusters closely aligned with concentrated postsynaptic receptors and scaffolding proteins4–6, suggesting a transsynaptic molecular “nanocolumn.””
From A trans-synaptic nanocolumn aligns neurotransmitter release to receptors (2016) · cites this paper as [6]
The Results section on subsynaptic nanodomains (Fig. 4F–H; page unavailable) shows postsynaptic PSD-95 nanodomains associated with AMPA receptors and apposed to presynaptic vGlut1 labeling. It does not identify presynaptic RIM nanoclusters or show that those clusters closely align with the postsynaptic proteins. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe alignment of pre- and postsynaptic nanoscale subdomains suggests that even small synapses may be composed of dynamic functional modules.
“The alignment of pre and postsynaptic nanoscale subdomains4–6 suggests that even small synapses may be composed of dynamic functional modules28,29.”
From A trans-synaptic nanocolumn aligns neurotransmitter release to receptors (2016) · cites this paper as [6]
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
A guide to choosing fluorescent proteins
Shaner, N. C., Steinbach, P. A., & Tsien, R. Y. (2005) · Nature Methods · doi:10.1038/nmeth819 · Cited by 2,823 · see citing works
Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
Miesenböck, G., Angelis, D. A. D., & Rothman, J. E. (1998) · Nature · doi:10.1038/28190 · Cited by 2,569 · see citing works
PDZ domain proteins of synapses
Kim, E., & Sheng, M. (2004) · Nature reviews. Neuroscience · doi:10.1038/nrn1517 · Cited by 1,565 · see citing works
PSD-95 Involvement in Maturation of Excitatory Synapses
El-Husseini, A. E.-D., Schnell, E., Chetkovich, D. M., Nicoll, R. A., & Bredt, D. S. (2000) · Science · doi:10.1126/science.290.5495.1364 · Cited by 1,303 · see citing works
Palmitoylation: policing protein stability and traffic
Linder, M. E., & Deschenes, R. J. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2084 · Cited by 1,192 · see citing works
Neurexins Induce Differentiation of GABA and Glutamate Postsynaptic Specializations via Neuroligins
Graf, E. R., Zhang, X., Jin, S., Linhoff, M. W., & Craig, A. M. (2004) · Cell · doi:10.1016/j.cell.2004.11.035 · Cited by 989 · see citing works
An Acylation Cycle Regulates Localization and Activity of Palmitoylated Ras Isoforms
Rocks, O., Peyker, A., Kahms, M., Verveer, P., Koerner, C., Lumbierres, M., Kuhlmann, J., Waldmann, H., Wittinghofer, A., & Bastiaens, P. (2005) · Science · doi:10.1126/science.1105654 · Cited by 866 · see citing works
Neuroligins Determine Synapse Maturation and Function
Varoqueaux, F., Aramuni, G., Rawson, R. L., Mohrmann, R., Missler, M., Gottmann, K., Zhang, W., Südhof, T. C., & Brose, N. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.003 · Cited by 818 · see citing works
Superresolution Imaging of Chemical Synapses in the Brain
Dani, A., Huang, B., Bergan, J. F., Dulac, C. G., & Zhuang, X. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.021 · Cited by 718 · see citing works
Control of Excitatory and Inhibitory Synapse Formation by Neuroligins
Chih, B., Engelman, H. S., & Scheiffele, P. (2005) · Science · doi:10.1126/science.1107470 · Cited by 707 · see citing works
Protein palmitoylation in neuronal development and synaptic plasticity
Fukata, Y., & Fukata, M. (2010) · Nature reviews. Neuroscience · doi:10.1038/nrn2788 · Cited by 614 · see citing works
Self-citationPhotoactivatable mCherry for high-resolution two-color fluorescence microscopy
Subach, F. V., Patterson, G. H., Manley, S., Gillette, J. M., Lippincott‐Schwartz, J., & Verkhusha, V. V. (2009) · Nature Methods · doi:10.1038/nmeth.1298 · Cited by 608 · see citing works
Synchronization of secretory protein traffic in populations of cells
Boncompain, G., Divoux, S., Gareil, N., de Forges, H., Lescure, A., Latreche, L., Mercanti, V., Jollivet, F., Raposo, G., & Perez, F. (2012) · Nature Methods · doi:10.1038/nmeth.1928 · Cited by 598 · see citing works
Self-citationSynaptic Strength Regulated by Palmitate Cycling on PSD-95
El-Husseini, A., Schnell, E., Dakoji, S., Sweeney, N. T., Zhou, Q., Prange, O., Gauthier-Campbell, C., Aguilera-Moreno, A., Nicoll, R. A., & Bredt, D. S. (2002) · Cell · doi:10.1016/s0092-8674(02)00683-9 · Cited by 569 · see citing works
Tomita, S., Chen, L., Kawasaki, Y., Petralia, R. S., Wenthold, R. J., Nicoll, R. A., & Bredt, D. S. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200212116 · Cited by 535 · see citing works
Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation
Kang, R., Wan, J., Arstikaitis, P., Takahashi, H., Huang, K., Bailey, A. O., Thompson, J. X., Roth, A. F., Drisdel, R. C., Mastro, R., et al. (2008) · Nature · doi:10.1038/nature07605 · Cited by 533 · see citing works
Identification of PSD-95 Palmitoylating Enzymes
Fukata, M., Fukata, Y., Adesnik, H., Nicoll, R. A., & Bredt, D. S. (2004) · Neuron · doi:10.1016/j.neuron.2004.12.005 · Cited by 532 · see citing works
Self-citationUltrastructure of dendritic spines: correlation between synaptic and spine morphologies
Arellano, J. I. (2007) · Frontiers in Neuroscience · doi:10.3389/neuro.01.1.1.010.2007 · Cited by 529 · see citing works
PSD-95 is required for activity-driven synapse stabilization.
Ehrlich, I., Klein, M., Rumpel, S., & Malinow, R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609307104 · Cited by 470 · see citing works
MEMBRANE-ASSOCIATED GUANYLATE KINASES REGULATE ADHESION AND PLASTICITY AT CELL JUNCTIONS
Funke, L., Dakoji, S., & Bredt, D. S. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133339 · Cited by 469 · see citing works
Dynamin-dependent endocytosis of ionotropic glutamate receptors
Carroll, R. C., Beattie, E. C., Xia, H., Lüscher, C., Altschuler, Y., Nicoll, R. A., Malenka, R. C., & von Zastrow, M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.14112 · Cited by 421 · see citing works
Palmitoylation of Ligands, Receptors, and Intracellular Signaling Molecules
Resh, M. D. (2006) · Science s STKE · doi:10.1126/stke.3592006re14 · Cited by 415 · see citing works
Elias, G. M., Funke, L., Stein, V., Grant, S., Bredt, D., & Nicoll, R. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.012 · Cited by 413 · see citing works
Synapse-specific regulation of AMPA receptor function by PSD-95.
Béïque, J.-C., Lin, D.-T., Kang, M.-G., Aizawa, H., Takamiya, K., & Huganir, R. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608492103 · Cited by 398 · see citing works
Rao, A., Kim, E., Sheng, M., & Craig, A. M. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-04-01217.1998 · Cited by 390 · see citing works
The intracellular dynamic of protein palmitoylation
Salaün, C., Greaves, J., & Chamberlain, L. H. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201008160 · Cited by 357 · see citing works
The postsynaptic density proteins Homer and Shank form a polymeric network structure
Hayashi, M. K., Tang, C., Verpelli, C., Narayanan, R., Stearns, M. H., Xu, R.-M., Li, H., Sala, C., & Hayashi, Y. (2009) · Cell · doi:10.1016/j.cell.2009.01.050 · Cited by 356 · see citing works
Protein palmitoylation: a regulator of neuronal development and function
El-Husseini, A., & Bredt, D. S. (2002) · Nature reviews. Neuroscience · doi:10.1038/nrn940 · Cited by 341 · see citing works
Synaptic Targeting of the Postsynaptic Density Protein PSD-95 Mediated by Lipid and Protein Motifs
Craven, S. E., El-Husseini, A., & Bredt, D. S. (1999) · Neuron · doi:10.1016/s0896-6273(00)80705-9 · Cited by 326 · see citing works
Postsynaptic assembly induced by neurexin-neuroligin interaction and neurotransmitter
Nam, C. I., & Chen, L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502038102 · Cited by 322 · see citing works
PSD-95 Is Required to Sustain the Molecular Organization of the Postsynaptic Density
Chen, X., Nelson, C. D., Li, X., Winters, C. A., Azzam, R. N., Sousa, A. A., Leapman, R. D., Gainer, H., Sheng, M., & Reese, T. S. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5968-10.2011 · Cited by 304 · see citing works
Topinka, J. R., & Bredt, D. S. (1998) · Neuron · doi:10.1016/s0896-6273(00)80440-7 · Cited by 302 · see citing works
Laminar Organization of the NMDA Receptor Complex within the Postsynaptic Density
Valtschanoff, J. G., & Weinberg, R. J. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-04-01211.2001 · Cited by 301 · see citing works
Synaptic trafficking of glutamate receptors by MAGUK scaffolding proteins
Elias, G. M., & Nicoll, R. A. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.07.005 · Cited by 288 · see citing works
Detection of GTP-Tubulin Conformation in Vivo Reveals a Role for GTP Remnants in Microtubule Rescues
Dimitrov, A., Quesnoit, M., Moutel, S., Cantaloube, I., Poüs, C., & Perez, F. (2008) · Science · doi:10.1126/science.1165401 · Cited by 273 · see citing works
Self-citationEl-Husseini, A., Craven, S. E., Chetkovich, D. M., Firestein, B. L., Schnell, E., Aoki, C. J., & Bredt, D. S. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.1.159 · Cited by 272 · see citing works
Dynamic Interaction of Stargazin-like TARPs with Cycling AMPA Receptors at Synapses
Tomita, S., Fukata, M., Nicoll, R. A., & Bredt, D. S. (2004) · Science · doi:10.1126/science.1090262 · Cited by 234 · see citing works
Self-citationMobile DHHC palmitoylating enzyme mediates activity-sensitive synaptic targeting of PSD-95
Noritake, J., Fukata, Y., Iwanaga, T., Hosomi, N., Tsutsumi, R., Matsuda, N., Tani, H., Iwanari, H., Mochizuki, Y., Kodama, T., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200903101 · Cited by 217 · see citing works
Self-citationNakagawa, T., Futai, K., Lashuel, H. A., Lo, I., Okamoto, K., Walz, T., Hayashi, Y., & Sheng, M. (2004) · Neuron · doi:10.1016/j.neuron.2004.10.012 · Cited by 214 · see citing works
Petersen, J. D., Chen, X., Vinadé, L., Döṣemeci, A., Lisman, J. E., & Reese, T. S. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-35-11270.2003 · Cited by 211 · see citing works
Kuriu, T., Inoue, A., Bito, H., Sobue, K., & Okabe, S. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0522-06.2006 · Cited by 206 · see citing works
Palmitoylation by DHHC5/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking
Thomas, G. M., Hayashi, T., Chen, C.-M., Chiu, S.-L., & Huganir, R. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.021 · Cited by 181 · see citing works
TARP Phosphorylation Regulates Synaptic AMPA Receptors through Lipid Bilayers
Sumioka, A., Yan, D., & Tomita, S. (2010) · Neuron · doi:10.1016/j.neuron.2010.04.035 · Cited by 167 · see citing works
Identification of G Protein α Subunit-Palmitoylating Enzyme
Tsutsumi, R., Fukata, Y., Noritake, J., Iwanaga, T., Perez, F., & Fukata, M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01144-08 · Cited by 139 · see citing works
Self-citationStructural plasticity with preserved topology in the postsynaptic protein network
Blanpied, T. A., Kerr, J. M., & Ehlers, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711669105 · Cited by 133 · see citing works
Recombinant Antibodies to the Small GTPase Rab6 as Conformation Sensors
Nizak, C., Monier, S., Nery, E. D., Moutel, S., Goud, B., & Perez, F. (2003) · Science · doi:10.1126/science.1083911 · Cited by 130 · see citing works
Self-citationNizak, C., Lluesma, S. M., Moutel, S., Roux, A., Kreis, T. E., Goud, B., & Perez, F. (2003) · Traffic · doi:10.1034/j.1600-0854.2003.00132.x · Cited by 113 · see citing works
Self-citationPickard, L., Noël, J., Duckworth, J. K., Fitzjohn, S. M., Henley, J. M., Collingridge, G. L., & Molnár, E. (2001) · Neuropharmacology · doi:10.1016/s0028-3908(01)00127-7 · Cited by 107 · see citing works
Shuttling of G Protein Subunits between the Plasma Membrane and Intracellular Membranes
Chisari, M., Saini, D. K., Kalyanaraman, V., & Gautam, N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704246200 · Cited by 98 · see citing works
Gorleku, O. A., Barns, A.-M., Prescott, G. R., Greaves, J., & Chamberlain, L. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.272369 · Cited by 82 · see citing works
Presynaptic Trafficking of Synaptotagmin I Is Regulated by Protein Palmitoylation
Kang, R., Swayze, R. D., Lisé, M.-F., Gerrow, K., Mullard, A., Honer, W. G., & El-Husseini, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404981200 · Cited by 80 · see citing works
Greaves, J., Carmichael, J. A., & Chamberlain, L. H. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-11-0924 · Cited by 75 · see citing works
A multi-Fc-species system for recombinant antibody production
Moutel, S., Marjou, A. E., Vielemeyer, O., Nizak, C., Benaroch, P., Dübel, S., & Perez, F. (2009) · BMC Biotechnology · doi:10.1186/1472-6750-9-14 · Cited by 65 · see citing works
Self-citationProtein modifications involved in neurotransmitter and gasotransmitter signaling
Sen, N., & Snyder, S. H. (2010) · Trends in Neurosciences · doi:10.1016/j.tins.2010.07.004 · Cited by 53 · see citing works
Structure and composition of the postsynaptic density during development
Swulius, M. T., Kubota, Y., Forest, A., & Waxham, M. N. (2010) · The Journal of Comparative Neurology · doi:10.1002/cne.22451 · Cited by 50 · see citing works
Lorenzon, N. M., Haarmann, C., Norris, E., Papadopoulos, S., & Beam, K. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405318200 · Cited by 27 · see citing works
Tagging of NS5A expressed from a functional hepatitis C virus replicon
McCormick, C. J., Maucourant, S., Griffin, S. D. C., Rowlands, D. J., & Harris, M. (2006) · Journal of General Virology · doi:10.1099/vir.0.81553-0 · Cited by 22 · see citing works
Characterization of single chain antibody targets through yeast two hybrid
Vielemeyer, O., Nizak, C., Jiménez, A. J., Échard, A., Goud, B., Camonis, J., Rain, J., & Perez, F. (2010) · BMC Biotechnology · doi:10.1186/1472-6750-10-59 · Cited by 21 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Fluorescence nanoscopy in cell biology
Sahl, S. J., Hell, S. W., & Jakobs, S. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.71 · Cited by 975 · see citing works
Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels
Hansen, K. B., Wollmuth, L. P., Bowie, D., Furukawa, H., Menniti, F. S., Sobolevsky, A. I., Swanson, G. T., Swanger, S. A., Greger, I. H., Nakagawa, T., et al. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000131 · Cited by 686 · see citing works
A trans-synaptic nanocolumn aligns neurotransmitter release to receptors
Tang, A.-H., Chen, H., Li, T. P., Metzbower, S. R., MacGillavry, H. D., & Blanpied, T. A. (2016) · Nature · doi:10.1038/nature19058 · Cited by 677 · see citing works
MINFLUX nanoscopy delivers 3D multicolor nanometer resolution in cells
Gwosch, K. C., Pape, J. K., Balzarotti, F., Hoess, P., Ellenberg, J., Ries, J., & Hell, S. W. (2020) · Nature Methods · doi:10.1038/s41592-019-0688-0 · Cited by 570 · see citing works
Choquet, D., & Triller, A. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.013 · Cited by 515 · see citing works
SR-Tesseler: a method to segment and quantify localization-based super-resolution microscopy data
Levet, F., Hosy, E., Kechkar, A., Butler, C., Beghin, A., Choquet, D., & Sibarita, J.-B. (2015) · Nature Methods · doi:10.1038/nmeth.3579 · Cited by 502 · see citing works
The Physiology of Protein S- acylation
Chamberlain, L. H., & Shipston, M. J. (2015) · Physiological Reviews · doi:10.1152/physrev.00032.2014 · Cited by 411 · see citing works
Ohkawa, T., Fukata, Y., Yamasaki, M., Miyazaki, T., Yokoi, N., Takashima, H., Watanabe, M., Watanabe, O., & Fukata, M. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3506-13.2013 · Cited by 352 · see citing works
Self-citationTranscellular Nanoalignment of Synaptic Function
Biederer, T., Kaeser, P. S., & Blanpied, T. A. (2017) · Neuron · doi:10.1016/j.neuron.2017.10.006 · Cited by 352 · see citing works
Lin, D. T. S., & Conibear, E. (2015) · eLife · doi:10.7554/elife.11306 · Cited by 333 · see citing works
Transmission of innate immune signaling by packaging of cGAMP in viral particles
Gentili, M., Kowal, J., Tkach, M., Satoh, T., Lahaye, X., Conrad, C., Boyron, M., Lombard, B., Durand, S., Kroemer, G., et al. (2015) · Science · doi:10.1126/science.aab3628 · Cited by 322 · see citing works
Chen, B., Sun, Y., Niu, J., Jarugumilli, G. K., & Wu, X. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.05.003 · Cited by 274 · see citing works
Palmitoylation of NOD1 and NOD2 is required for bacterial sensing
Lu, Y., Zheng, Y., Coyaud, É., Zhang, C., Selvabaskaran, A., Yu, Y., Xu, Z., Weng, X., Chen, J. S., Meng, Y., et al. (2019) · Science · doi:10.1126/science.aau6391 · Cited by 240 · see citing works
Mechanisms and functions of protein S-acylation
Mesquita, F. S., Abrami, L., Linder, M. E., Bamji, S. X., Dickinson, B. C., & van der Goot, F. G. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00700-8 · Cited by 231 · see citing works
Identification of PSD-95 Depalmitoylating Enzymes
Yokoi, N., Fukata, Y., Sekiya, A., Murakami, T., Kobayashi, K., & Fukata, M. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0419-16.2016 · Cited by 229 · see citing works
Self-citationMechanistic basis of MAGUK-organized complexes in synaptic development and signalling
Zhu, J., Shang, Y., & Zhang, M. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.18 · Cited by 209 · see citing works
Pre-post synaptic alignment through neuroligin-1 tunes synaptic transmission efficiency
Haas, K. T., Compans, B., Letellier, M., Bartol, T. M., Grillo-Bosch, D., Sejnowski, T. J., Sainlos, M., Choquet, D., Thoumine, O., & Hosy, E. (2018) · eLife · doi:10.7554/elife.31755 · Cited by 183 · see citing works
PSD95 nanoclusters are postsynaptic building blocks in hippocampus circuits
Broadhead, M. J., Horrocks, M. H., Zhu, F., Mureşan, L., Benavides‐Piccione, R., DeFelipe, J., Fricker, D. G., Kopanitsa, M. V., Duncan, R. R., Klenerman, D., et al. (2016) · Scientific Reports · doi:10.1038/srep24626 · Cited by 173 · see citing works
Willems, J., de Jong, A. P. H., Scheefhals, N., Mertens, E. J., Catsburg, L. A. E., Poorthuis, R. B., de Winter, F., Verhaagen, J., Meye, F. J., & MacGillavry, H. D. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000665 · Cited by 166 · see citing works
MAGUKs: multifaceted synaptic organizers
Won, S., Levy, J. M., Nicoll, R. A., & Roche, K. W. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.01.006 · Cited by 155 · see citing works
Functional organization of postsynaptic glutamate receptors
Scheefhals, N., & MacGillavry, H. D. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.05.002 · Cited by 151 · see citing works
Chazeau, A., Mehidi, A., Nair, D. K., Gautier, J. J., Leduc, C., Chamma, I., Kage, F., Kechkar, A., Thoumine, O. R., Rottner, K., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201488837 · Cited by 141 · see citing works
Choquet, D. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.2119-18.2018 · Cited by 141 · see citing works
Palmitoylation in Alzheimers disease and other neurodegenerative diseases
Cho, E., & Park, M. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.06.008 · Cited by 142 · see citing works
Compans, B., Camus, C., Kallergi, E., Sposini, S., Martineau, M., Butler, C., Kechkar, A., Klaassen, R. V., Retailleau, N., B, T. J. S. A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23133-9 · Cited by 136 · see citing works
Identification and Characterization of GABAA Receptor Autoantibodies in Autoimmune Encephalitis
Ohkawa, T., Satake, S., Yokoi, N., Miyazaki, Y., Ohshita, T., Sobue, G., Takashima, H., Watanabe, O., Fukata, Y., & Fukata, M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.4415-13.2014 · Cited by 131 · see citing works
Self-citationNanoscale Subsynaptic Domains Underlie the Organization of the Inhibitory Synapse
Crosby, K. C., Gookin, S. E., Garcia, J. D., Zent, K. H., Dell’Acqua, M. L., & Smith, K. R. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.070 · Cited by 126 · see citing works
Palmitoylation of δ-catenin by DHHC5 mediates activity-induced synapse plasticity
Brigidi, G. S., Sun, Y., Beccano-Kelly, D. A., Pitman, K. A., Mobasser, M., Borgland, S. L., Milnerwood, A. J., & Bamji, S. X. (2014) · Nature Neuroscience · doi:10.1038/nn.3657 · Cited by 122 · see citing works
Supramolecular organization of NMDA receptors and the postsynaptic density
Frank, R., & Grant, S. G. N. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.05.019 · Cited by 119 · see citing works
Robust nanoscopy of a synaptic protein in living mice by organic-fluorophore labeling
Masch, J.-M., Steffens, H., Fischer, J., Engelhardt, J., Hubrich, J., Keller‐Findeisen, J., D’Este, E., Urban, N. T., Grant, S. G. N., Sahl, S. J., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1807104115 · Cited by 119 · see citing works
Activity-regulated trafficking of the palmitoyl-acyl transferase DHHC5
Brigidi, G. S., Santyr, B. G., Shimell, J. J., Jovellar, D. B., & Bamji, S. X. (2015) · Nature Communications · doi:10.1038/ncomms9200 · Cited by 118 · see citing works
Purkey, A., & Dell’Acqua, M. L. (2020) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2020.00008 · Cited by 113 · see citing works
Protein Palmitoylation and Its Role in Bacterial and Viral Infections
Sobocińska, J., Roszczenko, P., Ciesielska, A., & Kwiatkowska, K. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2017.02003 · Cited by 117 · see citing works
Nanoscale co-organization and coactivation of AMPAR, NMDAR, and mGluR at excitatory synapses
Goncalves, J., Bartol, T. M., Camus, C., Levet, F., Menegolla, A. P., Sejnowski, T. J., Sibarita, J.-B., Vivaudou, M., Choquet, D., & Hosy, E. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1922563117 · Cited by 112 · see citing works
Advanced imaging and labelling methods to decipher brain cell organization and function
Choquet, D., Sainlos, M., & Sibarita, J. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00441-z · Cited by 111 · see citing works
Remodeling of the postsynaptic plasma membrane during neural development
Tułodziecka, K., Diaz-Rohrer, B. B., Farley, M. M., Chan, R., Paolo, G. D., Levental, K. R., Waxham, M. N., & Levental, I. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-06-0420 · Cited by 109 · see citing works
Palmitoylation of Gephyrin Controls Receptor Clustering and Plasticity of GABAergic Synapses
Dejanovic, B., Semtner, M., Ebert, S., Lamkemeyer, T., Neuser, F., Lüscher, B., Meier, J. C., & Schwarz, G. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001908 · Cited by 109 · see citing works
Engineering Extracellular Vesicles Enriched with Palmitoylated ACE2 as COVID‐19 Therapy
Xie, F., Su, P., Pan, T., Zhou, X., Li, H., Huang, H.-Z., Wang, A.-J., Wang, F.-W., Huang, J., Yan, H.-Y., et al. (2021) · Advances in Materials · doi:10.1002/adma.202103471 · Cited by 95 · see citing works
Protein S-palmitoylation and cancer
Yeste‐Velasco, M., Linder, M. E., & Lu, Y. (2015) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2015.06.004 · Cited by 100 · see citing works
Smeland, O. B., Shadrin, A. A., Bahrami, S., Broce, I., Tesli, M., Frei, O., Wirgenes, K. V., O’Connell, K. S., Krull, F., Bettella, F., et al. (2020) · Biological Psychiatry · doi:10.1016/j.biopsych.2020.01.026 · Cited by 100 · see citing works
AMPA Receptors as Therapeutic Targets for Neurological Disorders
Lee, K., Goodman, L., Fourie, C., Schenk, S., Leitch, B., & Montgomery, J. M. (2015) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2015.10.004 · Cited by 102 · see citing works
Neurodevelopmental Disorders Associated with PSD-95 and Its Interaction Partners
Levy, A. M., Gómez‐Puertas, P., & Tümer, Z. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23084390 · Cited by 98 · see citing works
Role of Palmitoylation of Postsynaptic Proteins in Promoting Synaptic Plasticity
Matt, L., Kim, K., Chowdhury, D., & Hell, J. W. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00008 · Cited by 96 · see citing works
Posttranslational Modifications Regulate the Postsynaptic Localization of PSD-95
Vallejo, D., Codocedo, J. F., & Inestrosa, N. C. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9745-1 · Cited by 94 · see citing works
Bennett, V., & Lorenzo, D. N. (2015) · Current topics in membranes · doi:10.1016/bs.ctm.2015.10.001 · Cited by 97 · see citing works
Fernández, E., Collins, M. O., Frank, R., Zhu, F., Kopanitsa, M. V., Nithianantharajah, J., Lemprière, S. A., Fricker, D. G., Elsegood, K. A., McLaughlin, C. L., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.09.045 · Cited by 88 · see citing works
Subsynaptic positioning of AMPARs by LRRTM2 controls synaptic strength
Ramsey, A. M., Tang, A., LeGates, T. A., Gou, X., Carbone, B. E., Thompson, S. M., Biederer, T., & Blanpied, T. A. (2021) · Science Advances · doi:10.1126/sciadv.abf3126 · Cited by 90 · see citing works
Fukata, Y., Chen, X., Chiken, S., Hirano, Y., Yamagata, A., Inahashi, H., Sanbo, M., Sano, H., Goto, T., Hirabayashi, M., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2022580118 · Cited by 91 · see citing works
Self-citationJeyifous, O., Lin, E. I., Chen, X., Antinone, S. E., Mastro, R., Drisdel, R. C., Reese, T. S., & Green, W. N. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612963113 · Cited by 89 · see citing works
Epilepsy and synaptic proteins
Fukata, Y., & Fukata, M. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.02.001 · Cited by 86 · see citing works
Self-citationHe, M., Abdi, K. M., & Bennett, V. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201401016 · Cited by 85 · see citing works
Subsynaptic spatial organization as a regulator of synaptic strength and plasticity
Chen, H., Tang, A., & Blanpied, T. A. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.05.004 · Cited by 84 · see citing works
Buonarati, O. R., Hammes, E. A., Watson, J. F., Greger, I. H., & Hell, J. W. (2019) · Science Signaling · doi:10.1126/scisignal.aar6889 · Cited by 81 · see citing works
Fortin, D. A., Tillo, S., Yang, G., Rah, J., Melander, J. B., Bai, S., Soler‐Cedeño, O., Qin, M., Zemelman, B. V., Guo, C., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.3888-14.2014 · Cited by 74 · see citing works
The zDHHC family of S-acyltransferases
Lemonidis, K., Werno, M. W., Greaves, J., Diez-Ardanuy, C., Sanchez-Perez, M. C., Salaün, C., Thomson, D. M., & Chamberlain, L. H. (2015) · Biochemical Society Transactions · doi:10.1042/bst20140270 · Cited by 78 · see citing works
Arc/Arg3.1 function in long‐term synaptic plasticity: Emerging mechanisms and unresolved issues
Zhang, H., & Bramham, C. R. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14958 · Cited by 71 · see citing works
Kaiser, P. D., Maier, J., Traenkle, B., Emele, F. E., & Rothbauer, U. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.04.019 · Cited by 75 · see citing works
α-Actinin Anchors PSD-95 at Postsynaptic Sites
Matt, L., Kim, K., Hergarden, A. C., Patriarchi, T., Malik, Z. A., Park, D. K., Chowdhury, D., Buonarati, O. R., Henderson, P. B., Gökçek-Saraç, Ç., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.01.036 · Cited by 75 · see citing works
Synaptic FUS accumulation triggers early misregulation of synaptic RNAs in a mouse model of ALS
Sahadevan, S., Hembach, K., Tantardini, E., Pérez‐Berlanga, M., Hruška-Plocháň, M., Megat, S., Weber, J., Schwarz, P., Dupuis, L., Robinson, M. D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23188-8 · Cited by 73 · see citing works
Age-dependent regulation of synaptic connections by dopamine D2 receptors
Jia, J., Zhao, J. W., Hu, Z., Lindberg, D. M., & Li, Z. (2013) · Nature Neuroscience · doi:10.1038/nn.3542 · Cited by 72 · see citing works
Phase separation as a mechanism for assembling dynamic postsynaptic density signalling complexes
Feng, Z., Chen, X., Zeng, M., & Zhang, M. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.12.001 · Cited by 68 · see citing works
Protein palmitoylation in the development and plasticity of neuronal connections
Globa, A. K., & Bamji, S. X. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.02.016 · Cited by 70 · see citing works
Patriarchi, T., Buonarati, O. R., & Hell, J. W. (2018) · The EMBO Journal · doi:10.15252/embj.201899771 · Cited by 65 · see citing works
Capping of the N‐terminus of PSD‐95 by calmodulin triggers its postsynaptic release
Zhang, Y., Matt, L., Patriarchi, T., Malik, Z. A., Chowdhury, D., Park, D. K., Renieri, A., Ames, J. B., & Hell, J. W. (2014) · The EMBO Journal · doi:10.1002/embj.201488126 · Cited by 68 · see citing works
Woolfrey, K. M., Sanderson, J. L., & Dell’Acqua, M. L. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2243-14.2015 · Cited by 69 · see citing works
Zhu, J., Zhou, Q., Shang, Y., Li, H., Peng, M., Ke, X., Weng, Z., Zhang, R., Huang, X., Li, S. S. C., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.11.107 · Cited by 68 · see citing works
Butland, S. L., Sanders, S. S., Schmidt, M. E., Riechers, S., Lin, D. T. S., Martin, D. D. O., Vaid, K., Graham, R. K., Singaraja, R. R., Wanker, E. E., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu137 · Cited by 65 · see citing works
Postsynaptic Neurotransmitter Receptor Reserve Pools for Synaptic Potentiation
Kneussel, M., & Hausrat, T. J. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.01.002 · Cited by 61 · see citing works
Purkey, A., Woolfrey, K. M., Crosby, K. C., Stich, D., Chick, W. S. H., Aoto, J. N., & Dell’Acqua, M. L. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.09.085 · Cited by 65 · see citing works
Ion channel regulation by protein S-acylation
Shipston, M. J. (2014) · The Journal of General Physiology · doi:10.1085/jgp.201411176 · Cited by 64 · see citing works
Diffusion dynamics of synaptic molecules during inhibitory postsynaptic plasticity
Petrini, E. M., & Barberis, A. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00300 · Cited by 62 · see citing works
Roles of two types of heparan sulfate clusters in Wnt distribution and signaling in Xenopus
Mii, Y., Yamamoto, T., Takada, R., Mizumoto, S., Matsuyama, M., Yamada, S., Takada, S., & Taira, M. (2017) · Nature Communications · doi:10.1038/s41467-017-02076-0 · Cited by 61 · see citing works
Local Palmitoylation Cycles and Specialized Membrane Domain Organization
Fukata, Y., Murakami, T., Yokoi, N., & Fukata, M. (2015) · Current topics in membranes · doi:10.1016/bs.ctm.2015.10.003 · Cited by 60 · see citing works
Self-citationStress-induced Changes in the S-palmitoylation and S-nitrosylation of Synaptic Proteins*[S]
Zaręba-Kozioł, M., Bartkowiak-Kaczmarek, A., Figiel, I., Krzystyniak, A., Wójtowicz, T., Bijata, M., & Włodarczyk, J. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001581 · Cited by 58 · see citing works
AMPA receptor nanoscale dynamic organization and synaptic plasticities
Choquet, D., & Hosy, E. (2020) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2020.04.003 · Cited by 59 · see citing works
Zaręba-Kozioł, M., Figiel, I., Bartkowiak, A., & Włodarczyk, J. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00175 · Cited by 59 · see citing works
Zinc Stabilizes Shank3 at the Postsynaptic Density of Hippocampal Synapses
Tao-Cheng, J.-H., Toy, D., Winters, C. A., Reese, T. S., & Döṣemeci, A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0153979 · Cited by 59 · see citing works
Activity Dependent and Independent Determinants of Synaptic Size Diversity
Hazan, L., & Ziv, N. E. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.2181-19.2020 · Cited by 61 · see citing works
Regulatory effects of post-translational modifications on zDHHC S-acyltransferases
Zmuda, F., & Chamberlain, L. H. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.014717 · Cited by 53 · see citing works
Targeting protein palmitoylation: selective inhibitors and implications in disease
Chavda, B., Arnott, J. A., & Planey, S. L. (2014) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2014.933802 · Cited by 52 · see citing works
Local and substrate-specific S-palmitoylation determines subcellular localization of Gαo
Solis, G. P., Kazemzadeh, A., Abrami, L., Valnohová, J., Álvarez, C., van der Goot, F. G., & Katanaev, V. L. (2022) · Nature Communications · doi:10.1038/s41467-022-29685-8 · Cited by 52 · see citing works
Mechanistic effects of protein palmitoylation and the cellular consequences thereof
Blašković, S., Adibekian, A., Blanc, M., & van der Goot, G. F. (2014) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2014.02.001 · Cited by 52 · see citing works
Homeostatic synaptic scaling: molecular regulators of synaptic AMPA-type glutamate receptors
Chowdhury, D., & Hell, J. W. (2018) · F1000Research · doi:10.12688/f1000research.13561.1 · Cited by 50 · see citing works
Live cell imaging of signaling and metabolic activities
Depaoli, M. R., Bischof, H., Eroğlu, E., Burgstaller, S., Ramadani‐Muja, J., Rauter, T., Schinagl, M., Waldeck‐Weiermair, M., Hay, J., Graier, W. F., et al. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.06.003 · Cited by 52 · see citing works
Shimell, J. J., Shah, B. S., Cain, S. M., Thouta, S., Kuhlmann, N., Tatarnikov, I., Jovellar, D. B., Brigidi, G. S., Kass, J., Milnerwood, A. J., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.10.065 · Cited by 52 · see citing works
Eisinger, K. R. T., Gross, K. S., Head, B. P., & Mermelstein, P. G. (2018) · Hormones and Behavior · doi:10.1016/j.yhbeh.2018.03.001 · Cited by 50 · see citing works
Moutin, E., Nikonenko, I., Stefanelli, T., Wirth, A., Ponimaskin, E. G., Roo, M. D., & Müller, D. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw183 · Cited by 49 · see citing works
Understanding the molecular diversity of synapses
van Oostrum, M., & Schuman, E. M. (2025) · Nature Reviews Neuroscience · doi:10.1038/s41583-024-00888-w · Cited by 49 · see citing works
Progress toward Understanding Protein S-acylation: Prospective in Plants
Li, Y., & Qi, B. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.00346 · Cited by 48 · see citing works
Sanders, S. S., Hernandez, L. M., Soh, H., Karnam, S., Walikonis, R. S., Tzingounis, A. V., & Thomas, G. M. (2020) · eLife · doi:10.7554/elife.56058 · Cited by 45 · see citing works
The role of S‐acylation in protein trafficking
Daniotti, J. L., Pedro, M. P., & Taubas, J. V. (2017) · Traffic · doi:10.1111/tra.12510 · Cited by 45 · see citing works
Murakami, G., Hojo, Y., Kato, A., Komatsuzaki, Y., Horie, S., Soma, M., Kim, J., & Kawato, S. (2017) · Journal of Neuroendocrinology · doi:10.1111/jne.12561 · Cited by 45 · see citing works
The Interactome of Palmitoyl-Protein Thioesterase 1 (PPT1) Affects Neuronal Morphology and Function
Sapir, T., Segal, M., Grigoryan, G., Hansson, K. M., James, P., Segal, M., & Reiner, O. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00092 · Cited by 45 · see citing works
Trans-synaptic LGI1–ADAM22–MAGUK in AMPA and NMDA receptor regulation
Fukata, Y., Hirano, Y., Miyazaki, Y., Yokoi, N., & Fukata, M. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108628 · Cited by 45 · see citing works
Self-citationSuzuki, M., Murakami, T., Cheng, J., Kano, H., Fukata, M., & Fujimoto, T. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-11-1504 · Cited by 44 · see citing works
Self-citationThe Nanoworld of the Tripartite Synapse: Insights from Super-Resolution Microscopy
Heller, J. P., & Rusakov, D. A. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00374 · Cited by 44 · see citing works
Roles of palmitoylation in structural long-term synaptic plasticity
Ji, B., & Skup, M. (2021) · Molecular Brain · doi:10.1186/s13041-020-00717-y · Cited by 43 · see citing works
Jia, L., Chisari, M., Maktabi, M. H., Sobieski, C. A., Zhou, H., Konopko, A. M., Martin, B. R., Mennerick, S. J., & Blumer, K. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.531475 · Cited by 44 · see citing works
Kang, R., Wang, L., Sanders, S. S., Zuo, K., Hayden, M. R., & Raymond, L. A. (2019) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2019.00003 · Cited by 43 · see citing works
Small Fluorogenic Amino Acids for Peptide‐Guided Background‐Free Imaging
Moliner, F. D., Konieczna, Z., Mendive‐Tapia, L., Saleeb, R. S., Morris, K., Gonzalez‐Vera, J. A., Kaizuka, T., Grant, S. G. N., Horrocks, M. H., & Vendrell, M. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202216231 · Cited by 42 · see citing works
- Authors
- Fukata, Y., Dimitrov, A., Boncompain, G., Vielemeyer, O., Perez, F., & Fukata, M.
- Affiliations
- National Institute for Physiological Sciences (JP)
- Centre National de la Recherche Scientifique (FR)
- Centre National de la Recherche Scientifique, Unité Mixte de Recherche 144 2 and 3
- Corresponding author
- Perez, Franck
- Fukata, Masaki
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2013-07-08
- Volume
- 202
- Issue
- 1
- Pages
- 145-161
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC3704990
- OpenAlex
- W2168234829
- Cited by
- 262
- References
- 58
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 23 · 2023: 12 · 2022: 20 · 2021: 28 · 2020: 24 · 2019: 21 · 2018: 23 · 2017: 27 · 2016: 20 · 2015: 20 · 2014: 17 · 2013: 6
- FWCI
- 10.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Agence Nationale de la Recherche (ANR-09-BLAN-0290)
- Japan Society for the Promotion of Science
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- palmitoylation, PSD-95, postsynaptic density, dendritic spines, plasma membrane targeting, synaptic organization
- MeSH terms
- Disks Large Homolog 4 Protein, Animals, Chlorocebus aethiops, Fluorescent Dyes, Hippocampus, Humans, Membrane Proteins, Synaptic Transmission, Neuronal Plasticity, Neurons, Palmitates, Sensitivity and Specificity, Structure-Activity Relationship, Transfection, COS Cells, Dendritic Spines, Green Fluorescent Proteins, Mice, Rats, Guanylate Kinases, Lipoylation, HEK293 Cells, Post-Synaptic Density
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
