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Proteomics. 2015 Dec;15(23-24):4080-95. doi: 10.1002/pmic.201500159. Epub 2015 Sep 7.

Phosphoproteomic network analysis in the sea urchin Strongylocentrotus purpuratus reveals new candidates in egg activation.

Author information

1
Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, ON, Canada.
2
Department of Ecology, Evolution and Marine Biology, UC Santa Barbara, Santa Barbara, CA, USA.
3
Department of Molecular, Cellular and Developmental Biology, and Marine Science Institute, Santa Barbara, CA, USA.
4
Collaborative Innovation Center of Chinese Medicinal Resources Industrialization, College of Pharmacy, Nanjing University of Chinese Medicine, Nanjing, P. R. China.

Abstract

Fertilization triggers a dynamic symphony of molecular transformations induced by a rapid rise in intracellular calcium. Most prominent are surface alterations, metabolic activation, cytoskeletal reorganization, and cell-cycle reentry. While the activation process appears to be broadly evolutionarily conserved, and protein phosphorylation is known to play a key role, the signaling networks mediating the response to fertilization are not well described. To address this gap, we performed a time course phosphoproteomic analysis of egg activation in the sea urchin Strongylocentrotus purpuratus, a system that offers biochemical tractability coupled with exquisite synchronicity. By coupling large-scale phosphopeptide enrichment with unbiased quantitative MS, we identified striking changes in global phosphoprotein patterns at 2- and 5-min postfertilization as compared to unfertilized eggs. Overall, we mapped 8796 distinct phosphosite modifications on 2833 phosphoproteins, of which 15% were differentially regulated in early egg activation. Activated kinases were identified by phosphosite mapping, while enrichment analyses revealed conserved signaling cascades not previously associated with egg activation. This work represents the most comprehensive study of signaling associated with egg activation to date, suggesting novel mechanisms that can be experimentally tested and providing a valuable resource for the broader research community. All MS data have been deposited in the ProteomeXchange with identifier PXD002239 (http://proteomecentral.proteomexchange.org/dataset/PXD002239).

KEYWORDS:

Animal proteomics; Calcium; Egg activation; Network analysis; Phosphoproteomics

PMID:
26227301
DOI:
10.1002/pmic.201500159
[Indexed for MEDLINE]

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