Quantitative proteomics reveals the dynamics of protein changes during Drosophila oocyte maturation and the oocyte-to-embryo transition
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Kronja-2014-Quantitative proteom.pdf
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Author(s)
Kronja, Iva
Whitfield, Zachary J.
Yuan, Bingbing
Dzeyk, Kristina
Kirkpatrick, Joanna
Krijgsveld, Jeroen
Orr-Weaver, Terry
Date Issued
November 2014
Journal
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences (U.S.)
Citation
Kronja, Iva, Zachary J. Whitfield, Bingbing Yuan, Kristina Dzeyk, Joanna Kirkpatrick, Jeroen Krijgsveld, and Terry L. Orr-Weaver. “Quantitative Proteomics Reveals the Dynamics of Protein Changes During Drosophila Oocyte Maturation and the Oocyte-to-Embryo Transition.” Proceedings of the National Academy of Sciences 111, no. 45 (October 27, 2014): 16023–16028.
Version
Final published version
Abstract
The onset of development is marked by two major, posttranscriptionally controlled, events: oocyte maturation (release of the prophase I primary arrest) and egg activation (release from the secondary meiotic arrest). Using quantitative mass spectrometry, we previously described proteome remodeling during Drosophila egg activation. Here, we describe our quantitative mass spectrometry-based analysis of the changes in protein levels during Drosophila oocyte maturation. This study presents the first quantitative survey, to our knowledge, of proteome changes accompanying oocyte maturation in any organism and provides a powerful resource for identifying both key regulators and biological processes driving this critical developmental window. We show that Muskelin, found to be up-regulated during oocyte maturation, is required for timely nurse cell nuclei clearing from mature egg chambers. Other proteins up-regulated at maturation are factors needed not only for late oogenesis but also completion of meiosis and early embryogenesis. Interestingly, the down-regulated proteins are predominantly involved in RNA processing, translation, and RNAi. Integrating datasets on the proteome changes at oocyte maturation and egg activation uncovers dynamics in proteome remodeling during the change from oocyte to embryo. Notably, 66 proteins likely act uniquely during late oogenesis, because they are up-regulated at maturation and down-regulated at activation. We find down-regulation of this class of proteins to be mediated partially by APC/C[superscript CORT], a meiosis-specific form of the E3 ligase anaphase promoting complex/cyclosome (APC/C).
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
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DOI of Published Version
https://doi.org/10.1073/pnas.1418657111
