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    Protein Composition of Immunoprecipitated Synaptic Ribbons
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    † Eaton-Peabody Laboratory, Department of Otology and Laryngology, Massachusetts Eye and Ear Infirmary and Harvard Medical School, 243 Charles Street, Boston, Massachusetts 02114, United States
    ‡ Harvard Mass Spectrometry and Proteomics Resource Lab, FAS Center for Systems Biology, Harvard University, Cambridge, Massachusetts 02138, United States
    *William F. Sewell, Eaton-Peabody Laboratory, Massachusetts Eye and Ear Infirmary, 243 Charles Street, Boston, MA 02114. Phone: 617-573-3156. Fax: 617-720-4408. E-mail: [email protected]
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    Journal of Proteome Research

    Cite this: J. Proteome Res. 2012, 11, 2, 1163–1174
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    https://doi.org/10.1021/pr2008972
    Published November 21, 2011
    Copyright © 2011 American Chemical Society
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    Abstract

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    The synaptic ribbon is an electron-dense structure found in hair cells and photoreceptors. The ribbon is surrounded by neurotransmitter-filled vesicles and considered to play a role in vesicle release. We generated an objective, quantitative analysis of the protein composition of the ribbon complex using a mass spectrometry-based proteomics analysis. Our use of affinity-purified ribbons and control IgG immunoprecipitations ensure that the identified proteins are indeed associated with the ribbon complex. The use of mouse tissue, where the proteome is complete, generated a comprehensive analysis of the candidates. We identified 30 proteins (comprising 56 isoforms and subunits) associated with the ribbon complex. The ribbon complex primarily comprises proteins found in conventional synapses, which we categorized into 6 functional groups: vesicle handling (38.5%), scaffold (7.3%), cytoskeletal molecules (20.6%), phosphorylation enzymes (10.6%), molecular chaperones (8.2%), and transmembrane proteins from the presynaptic membrane firmly attached to the ribbon (11.3%). The 3 CtBP isoforms represent the major protein in the ribbon whether calculated by molar amount (30%) or by mass (20%). The relatively high quantity of phosphorylation enzymes suggests a very active and regulated structure. The ribbon appears to comprise a concentrated cluster of proteins dealing with vesicle creation, retention and distribution, and consequent exocytosis.

    Copyright © 2011 American Chemical Society

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    Journal of Proteome Research

    Cite this: J. Proteome Res. 2012, 11, 2, 1163–1174
    Click to copy citationCitation copied!
    https://doi.org/10.1021/pr2008972
    Published November 21, 2011
    Copyright © 2011 American Chemical Society
    Request reuse permissions

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