Evolution of complexity in the zebrafish synapse proteome.
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ICR Authors
Authors
Bayés, À
Collins, MO
Reig-Viader, R
Gou, G
Goulding, D
Izquierdo, A
Choudhary, JS
Emes, RD
Grant, SGN
Collins, MO
Reig-Viader, R
Gou, G
Goulding, D
Izquierdo, A
Choudhary, JS
Emes, RD
Grant, SGN
Document Type
Journal Article
Date
2017-03-02
Date Accepted
2017-01-15
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.
Citation
Nature communications, 2017, 8 pp. 14613 - ?
Source Title
Publisher
NATURE PORTFOLIO
ISSN
2041-1723
eISSN
2041-1723