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ZFIN ID: ZDB-PUB-170303-4
Evolution of complexity in the zebrafish synapse proteome
Bayés, À., Collins, M.O., Reig-Viader, R., Gou, G., Goulding, D., Izquierdo, A., Choudhary, J.S., Emes, R.D., Grant, S.G.
Date: 2017
Source: Nature communications 8: 14613 (Journal)
Registered Authors:
Keywords: Molecular evolution, Molecular neuroscience, Proteomics
MeSH Terms:
  • Animals
  • Brain/metabolism*
  • Brain/ultrastructure
  • Female
  • Gene Duplication
  • Genome
  • Male
  • Mice
  • Microscopy, Electron, Transmission
  • Models, Biological
  • Nerve Tissue Proteins/genetics
  • Nerve Tissue Proteins/metabolism*
  • Post-Synaptic Density/metabolism
  • Proteome/genetics
  • Proteome/metabolism*
  • Proteome/ultrastructure*
  • Species Specificity
  • Synapses/metabolism*
  • Synapses/ultrastructure
  • Synaptosomes/metabolism
  • Zebrafish
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism*
PubMed: 28252024 Full text @ Nat. Commun.
FIGURES
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.
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