title: Evolution of complexity in the zebrafish synapse proteome.
abstract: The proteome of human brain synapses is highly complex and is mutated in over 130 diseases. This complexity arose from two whole-genome duplications early in the vertebrate lineage. Zebrafish are used in modelling human diseases; however, its synapse proteome is uncharacterized, and whether the teleost-specific genome duplication (TSGD) influenced complexity is unknown. We report the characterization of the proteomes and ultrastructure of central synapses in zebrafish and analyse the importance of the TSGD. While the TSGD increases overall synapse proteome complexity, the postsynaptic density (PSD) proteome of zebrafish has lower complexity than mammals. A highly conserved set of ∼1,000 proteins is shared across vertebrates. PSD ultrastructural features are also conserved. Lineage-specific proteome differences indicate that vertebrate species evolved distinct synapse types and functions. The data sets are a resource for a wide range of studies and have important implications for the use of zebrafish in modelling human synaptic diseases.
authors.affiliation: Molecular Physiology of the Synapse Laboratory, Biomedical Research Institute Sant Pau (IIB Sant Pau), Sant Antoni Maria Claret 167, 08025 Barcelona, Spain.|Universitat Autònoma de Barcelona, Cerdanyola del Vallès, 08193 Bellaterra, Spain.
authors.forename: Àlex
authors.initials: À
authors.lastname: Bayés
authors.affiliation: Department of Biomedical Science, The Centre for Membrane Interactions and Dynamics, University of Sheffield, Western Bank, Sheffield S10 2TN, UK.
authors.forename: Mark O
authors.identifier: 0000-0002-7656-4975
authors.initials: MO
authors.lastname: Collins
authors.affiliation: Molecular Physiology of the Synapse Laboratory, Biomedical Research Institute Sant Pau (IIB Sant Pau), Sant Antoni Maria Claret 167, 08025 Barcelona, Spain.|Universitat Autònoma de Barcelona, Cerdanyola del Vallès, 08193 Bellaterra, Spain.
authors.forename: Rita
authors.initials: R
authors.lastname: Reig-Viader
authors.affiliation: Molecular Physiology of the Synapse Laboratory, Biomedical Research Institute Sant Pau (IIB Sant Pau), Sant Antoni Maria Claret 167, 08025 Barcelona, Spain.|Universitat Autònoma de Barcelona, Cerdanyola del Vallès, 08193 Bellaterra, Spain.
authors.forename: Gemma
authors.initials: G
authors.lastname: Gou
authors.affiliation: Pathogen Genomics, Wellcome Trust Sanger Institute, Hinxton CB10 1SA, UK.
authors.forename: David
authors.initials: D
authors.lastname: Goulding
authors.affiliation: School of Veterinary Medicine and Science, University of Nottingham. Sutton Bonington Campus, Leicestershire LE12 5RD, UK.
authors.forename: Abril
authors.initials: A
authors.lastname: Izquierdo
authors.affiliation: Proteomic Mass Spectrometry, The Wellcome Trust Sanger Institute, Hinxton, Cambridgeshire CB10 1SA, UK.
authors.forename: Jyoti S
authors.initials: JS
authors.lastname: Choudhary
authors.affiliation: School of Veterinary Medicine and Science, University of Nottingham. Sutton Bonington Campus, Leicestershire LE12 5RD, UK.|Advanced Data Analysis Centre, University of Nottingham, Sutton Bonington Campus, Leicestershire LE12 5RD, UK.
authors.forename: Richard D
authors.identifier: 0000-0001-6855-5481
authors.initials: RD
authors.lastname: Emes
authors.affiliation: Genes to Cognition Programme, Centre for Clinical Brain Science, University of Edinburgh, Edinburgh EH16 4SB, UK.
authors.forename: Seth G N
authors.initials: SG
authors.lastname: Grant
mesh_terms: D000818:Animals; D001921:Brain / Q000378:metabolism* / Q000648:ultrastructure; D005260:Female; D020440:Gene Duplication; D016678:Genome; D008297:Male; D051379:Mice; D046529:Microscopy, Electron, Transmission; D008954:Models, Biological; D009419:Nerve Tissue Proteins / Q000235:genetics / Q000378:metabolism*; D057907:Post-Synaptic Density / Q000378:metabolism; D020543:Proteome / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure*; D013045:Species Specificity; D013569:Synapses / Q000378:metabolism* / Q000648:ultrastructure; D013574:Synaptosomes / Q000378:metabolism; D015027:Zebrafish; D029961:Zebrafish Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D009419:Nerve Tissue Proteins; D020543:Proteome; D029961:Zebrafish Proteins