2DE identification of proteins exhibiting turnover and phosphorylation dynamics during sea urchin egg activation.

Title2DE identification of proteins exhibiting turnover and phosphorylation dynamics during sea urchin egg activation.
Publication TypeJournal Article
Year of Publication2008
AuthorsRoux MM, Radeke MJ, Goel M, Mushegian A, Foltz KR
JournalDev Biol
Volume313
Issue2
Pagination630-47
Date Published2008 Jan 15
ISSN1095-564X
KeywordsAnimals, Electrophoresis, Gel, Two-Dimensional, Female, Fertilization, Genome, Isoelectric Point, Male, Models, Biological, Ovum, Phosphoproteins, Phosphorylation, Proteome, Proteomics, Reproducibility of Results, Sea Urchins, Sperm-Ovum Interactions, Spermatozoa, Tandem Mass Spectrometry
Abstract

The animal egg is a unique quiescent cell, prepackaged with maternal mRNAs and proteins that have functions in early development. Rapid, transient signaling at fertilization alters egg physiology, resulting in Ca(2+) release from the endoplasmic reticulum (ER) and cytoplasmic alkalinization. These events trigger the zygote developmental program through initiation of DNA synthesis and entry into mitosis. Post-translational modifications of maternal proteins are responsible for the spatio-temporal regulation that orchestrates egg activation. We used functional proteomics to identify the candidate maternal proteins involved in egg activation and early development. As the first step of this analysis, we present the data on the baseline maternal proteome, in particular, on proteins exhibiting changes in abundance and in phosphorylation state upon egg activation. We identify 94 proteins that were stable, reproducibly displayed a shift in isoelectric point, or changed in relative abundance at specific times after activation. The identities of these proteins were determined by quadrupole time-of-flight tandem mass spectrometry. The set of the most dynamic proteins appear to be enriched in intermediary metabolism proteins, cytoskeletal proteins, gamete associated proteins and proteins that have Ca(2+) mediated activities.

DOI10.1016/j.ydbio.2007.10.053
Alternate JournalDev. Biol.
PubMed ID18082677