The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
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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Beausoleil, S. A., Villén, J., Gerber, S. A., Rush, J., & Gygi, S. P. (2006) · Nature Biotechnology · doi:10.1038/nbt1240 · Cited by 1,577
Adherens and tight junctions: Structure, function and connections to the actin cytoskeleton
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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
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