Show simple item record

dc.contributor.authorKronja, Iva
dc.contributor.authorWhitfield, Zachary J.
dc.contributor.authorYuan, Bingbing
dc.contributor.authorDzeyk, Kristina
dc.contributor.authorKirkpatrick, Joanna
dc.contributor.authorKrijgsveld, Jeroen
dc.contributor.authorOrr-Weaver, Terry
dc.date.accessioned2015-05-11T14:29:37Z
dc.date.available2015-05-11T14:29:37Z
dc.date.issued2014-11
dc.date.submitted2014-07
dc.identifier.issn0027-8424
dc.identifier.issn1091-6490
dc.identifier.urihttp://hdl.handle.net/1721.1/96955
dc.description.abstractThe 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).en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (Grant GM39341)en_US
dc.language.isoen_US
dc.publisherNational Academy of Sciences (U.S.)en_US
dc.relation.isversionofhttp://dx.doi.org/10.1073/pnas.1418657111en_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.sourceNational Academy of Sciences (U.S.)en_US
dc.titleQuantitative proteomics reveals the dynamics of protein changes during Drosophila oocyte maturation and the oocyte-to-embryo transitionen_US
dc.typeArticleen_US
dc.identifier.citationKronja, 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.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.departmentWhitehead Institute for Biomedical Researchen_US
dc.contributor.mitauthorWhitfield, Zachary J.en_US
dc.contributor.mitauthorOrr-Weaver, Terry L.en_US
dc.relation.journalProceedings of the National Academy of Sciencesen_US
dc.eprint.versionFinal published versionen_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsKronja, Iva; Whitfield, Zachary J.; Yuan, Bingbing; Dzeyk, Kristina; Kirkpatrick, Joanna; Krijgsveld, Jeroen; Orr-Weaver, Terry L.en_US
dc.identifier.orcidhttps://orcid.org/0000-0002-7934-111X
mit.licensePUBLISHER_POLICYen_US
mit.metadata.statusComplete


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record