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Proteomic Analysis of in Vivo Phosphorylated Synaptic Proteins
Open accessAbstract
In the nervous system, protein phosphorylation is an essential feature of synaptic function. Although protein phosphorylation is known to be important for many synaptic processes and in disease, little is known about global phosphorylation of synaptic proteins. Heterogeneity and low abundance make protein phosphorylation analysis difficult, particularly for mammalian tissue samples. Using a new approach, combining both protein and peptide immobilized metal affinity chromatography and mass spectrometry data acquisition strategies, we have produced the first large scale map of the mouse synapse phosphoproteome. We report over 650 phosphorylation events corresponding to 331 sites (289 have been unambiguously assigned), 92% of which are novel. These represent 79 proteins, half of which are novel phosphoproteins, and include several highly phosphorylated proteins such as MAP1B (33 sites) and Bassoon (30 sites). An additional 149 candidate phosphoproteins were identified by profiling the composition of the protein immobilized metal affinity chromatography enrichment. All major synaptic protein classes were observed, including components of important pre- and postsynaptic complexes as well as low abundance signaling proteins. Bioinformatic and in vitro phosphorylation assays of peptide arrays suggest that a small number of kinases phosphorylate many proteins and that each substrate is phosphorylated by many kinases. These data substantially increase existing knowledge of synapse pro…
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“It should be pointed out that, although it is well established that CaMKII phosphorylates numerous synaptic proteins (66, 434–437), as reviewed here, despite intensive research an essential role for CaMKII phosphorylation of many of these targets largely remains elusive.”
From Synaptic memory and CaMKII (2023) · cites this paper as [436]
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Cites
Südhof, T. C. (2004) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.041002.131412 · Cited by 2,491
Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae
Ficarro, S. B., McCleland, M. L., Stukenberg, P. T., Burke, D. J., Ross, M. M., Shabanowitz, J., Hunt, D. F., & White, F. M. (2002) · Nature Biotechnology · doi:10.1038/nbt0302-301 · Cited by 1,636
Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs
Obenauer, J. C. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg584 · Cited by 1,609
Large-scale characterization of HeLa cell nuclear phosphoproteins
Beausoleil, S. A., Jedrychowski, M. P., Schwartz, D., Elias, J. E., Villén, J., Li, J., Cohn, M. A., Cantley, L. C., & Gygi, S. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404720101 · Cited by 1,376
Synaptic Vesicle Phosphoproteins and Regulation of Synaptic Function
Greengard, P., Valtorta, F., Czernik, A. J., & Benfenati, F. (1993) · Science · doi:10.1126/science.8430330 · Cited by 1,311
Proteomic analysis of NMDA receptor–adhesion protein signaling complexes
Husi, H., Ward, M. A., Choudhary, J. S., Blackstock, W. P., & Grant, S. G. N. (2000) · Nature Neuroscience · doi:10.1038/76615 · Cited by 1,194
Self-citationTu, J. C., Xiao, B., Yuan, J. P., Lanahan, A. A., Leoffert, K., Li, M., Linden, D. J., & Worley, P. F. (1998) · Neuron · doi:10.1016/s0896-6273(00)80589-9 · Cited by 862
Carlin, R. K., Grab, D. J., Cohen, R. S., & Siekevitz, P. (1980) · The Journal of Cell Biology · doi:10.1083/jcb.86.3.831 · Cited by 788
Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography
Andersson, L., & Porath, J. O. (1986) · Analytical Biochemistry · doi:10.1016/0003-2697(86)90523-3 · Cited by 774
Cruz, J. C., Tseng, H.-C., Goldman, J. A., Shih, H., & Tsai, L.-H. (2003) · Neuron · doi:10.1016/s0896-6273(03)00627-5 · Cited by 609
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Giorgianni, F., Zhao, Y., Desiderio, D. M., & Beranová-Giorgianni, Š. (2007) · Electrophoresis · doi:10.1002/elps.200600782 · Cited by 22
Synapse proteomics: current status and quantitative applications
Li, K. W., & Jiménez, C. R. (2008) · Expert Review of Proteomics · doi:10.1586/14789450.5.2.353 · Cited by 23
Recent advances in neuroproteomics.
Andrade, E. C., Krueger‐Burg, D., & Nairn, A. C. (2007) · PubMed · Cited by 22
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Ramser, E. M., Buck, F., Schachner, M., & Tilling, T. (2010) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2010.05.013 · Cited by 21
Emes, R. D., & Grant, S. G. N. (2011) · Frontiers in Neuroscience · doi:10.3389/fnins.2011.00044 · Cited by 22
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Morón, J. A., & Devi, L. A. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04536.x · Cited by 19
Comparison of simple sucrose and percoll based methodologies for synaptosome enrichment
Tenreiro, P., Rebelo, S., Martins, F., Santos, M., Coelho, E. D. S., Almeida, M., Matos, A., & Silva, O. A. B. D. C. E. (2016) · Analytical Biochemistry · doi:10.1016/j.ab.2016.10.015 · Cited by 20
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Warthaka, M., Karwowska-Desaulniers, P., & Pflum, M. K. H. (2006) · ACS Chemical Biology · doi:10.1021/cb6003564 · Cited by 20
Subcellular Fractionation of the Brain: Preparation of Synaptosomes and Synaptic VesiclesPreprint
Evans, G. J. (2015) · Cold Spring Harbor Protocols · doi:10.1101/pdb.prot083469 · Cited by 20
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Papa, L. (2012) · InTech eBooks · doi:10.5772/31776 · Cited by 19
Aryal, U. K., Olson, D. J. H., & Ross, A. R. S. (2008) · PubMed Central · Cited by 19
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Molecular Diversity of Glutamatergic and GABAergic Synapses from Multiplexed Fluorescence Imaging
Danielson, E., de Arce, K. P., Cimini, B. A., Wamhoff, E., Singh, S., Cottrell, J. R., Carpenter, A. E., & Bathe, M. (2020) · eNeuro · doi:10.1523/eneuro.0286-20.2020 · Cited by 17
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Roohi, J., Tegay, D. H., Pomeroy, J. C., Burkett, S. S., Stone, G. A., Stanyon, R., & Hatchwell, E. (2008) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.30755 · Cited by 18
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Schein, S., & Ahmad, K. M. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.091744 · Cited by 12
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Lonardoni, F., & Maria, A. (2012) · InTech eBooks · doi:10.5772/32451 · Cited by 1
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Metadata
- Authors
- Collins, M. O., Yu, L., Coba, M. P., Husi, H., Campuzano, I., Blackstock, W. P., Choudhary, J. S., & Grant, S. G. N.
- Affiliations
- Wellcome Sanger Institute (GB)
- University of Edinburgh (GB)
- Waters (United Kingdom) (GB)
- University of Sheffield (GB)
- Corresponding author
- Grant, Seth G.N.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-02
- Volume
- 280
- Issue
- 7
- Pages
- 5972-5982
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2167791125
- Cited by
- 320
- References
- 43
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 2 · 2023: 7 · 2022: 4 · 2021: 11 · 2020: 6 · 2019: 11 · 2018: 9 · 2017: 8 · 2016: 12 · 2015: 8 · 2014: 11 · 2013: 9 · 2012: 17
- FWCI
- 14.96
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- 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
- Keywords
- synaptic proteins, protein phosphorylation, immobilized metal affinity chromatography, MAP1B, bassoon, kinase substrate specificity
- MeSH terms
- Animals, Cell Membrane, Phosphoproteins, Phosphorylation, Protein Binding, Protein Kinases, Solubility, Synapses, Synaptosomes, Urea, Computational Biology, Protein Array Analysis, Proteomics, Mice
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 ›
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