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Cited by 56Advanced Proteomics Techniques and ApplicationsNeuroscience and Neuropharmacology ResearchMass Spectrometry Techniques and Applications

Phosphoproteomic Analysis of Synaptosomes from Human Cerebral Cortex

DeGiorgis, Joseph A., Jaffe, Howard, Moreira, Jorge E., Carlotti, Carlos G., Leite, João P., Pant, Harish C., Dosemeci, Ayse·2005·Journal of Proteome Research
DOI 10.1021/pr0498436
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Abstract

Protein phosphorylation is a crucial post-translational modification mechanism in the regulation of synaptic organization and function. Here, we analyzed synaptosome fractions from human cerebral cortex obtained during therapeutic surgery. To minimize changes in the phosphorylation state of proteins, the tissue was homogenized within two minutes of excision. Synaptosomal proteins were digested with trypsin and phosphopeptides were isolated by immobilized metal affinity chromatography and analyzed by liquid chromatography and tandem mass spectrometry. The method allowed the detection of residues on synaptic proteins that were presumably phosphorylated in the intact cell, including synapsin 1, syntaxin 1, and SNIP, PSD-93, NCAM, GABA-B receptor, chaperone molecules, and protein kinases. Some of the residues identified are the same or homologous to sites that had been previously described to be phosphorylated in mammals whereas others appear to be novel sites which, to our knowledge, have not been reported previously. The study shows that new phosphoproteomic strategies can be used to analyze subcellular fractions from small amounts of tissue for the identification of phosphorylated residues for research and potentially for diagnostic purposes.

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Crossref · 10.1021/pr0498436

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  • Although it is well established that CaMKII phosphorylates numerous synaptic proteins, an essential role for CaMKII phosphorylation of many of these targets largely remains elusive.

    “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 [437]

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Authors
DeGiorgis, J. A., Jaffe, H., Moreira, J. E., Carlotti, C. G., Leite, J. P., Pant, H. C., & Dosemeci, A.
Affiliations
  • National Institutes of Health (US)
  • Laboratory of Neurobiology, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, Protein and Peptide Sequencing Facility, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, Department of Cellular and Molecular Biology, Ribeirão Preto School of Medicine, University of São Paulo, Ribeirão Preto, SP, Brasil, Division of Neurosurgery, Department of Surgery, Ribeirão Preto School of Medicine,...
ORCID
Venue
Journal of Proteome Research
Publisher
American Chemical Society (ACS)
Published
2005-02-05
Volume
4
Issue
2
Pages
306-315
ISSN
  • 1535-3893 (ISSN-L)
  • 1535-3907
DOI
10.1021/pr0498436
OpenAlex
W1985297803
Cited by
56
References
32
Citations by year
2023: 1 · 2021: 2 · 2020: 4 · 2019: 1 · 2018: 1 · 2017: 1 · 2015: 2 · 2014: 2 · 2013: 5 · 2012: 4
FWCI
3.62
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Proteome Research (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
Keywords
protein phosphorylation, synaptosomes, human cerebral cortex, synaptic proteins, synapsin-1, syntaxin-1, SNIP, PSD-93, CD56, GABAB receptors, protein kinases, molecular chaperones, post-translational modification
MeSH terms
Amino Acid Sequence, Cerebral Cortex, Humans, Molecular Sequence Data, Phosphoproteins, Substrate Specificity, Calcium-Calmodulin-Dependent Protein Kinases, Proline-Directed Protein Kinases, Proteomics, Calcium-Calmodulin-Dependent Protein Kinase Type 2

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