PXD020916-1
PXD020916 is an original dataset announced via ProteomeXchange.
Dataset Summary
Title | Selective dephosphorylation by PP2A-B55 directs the meiosis I - meiosis II transition in oocytes |
Description | Meiosis is a specialized cell cycle that requires sequential changes to the cell division machinery to facilitate changing functions. To define the mechanisms that enable the oocyte-to-embryo transition, we performed time-course proteomics in sea star oocytes from prophase I through the first embryonic cleavage. Although protein levels are broadly stable, dynamic waves of phosphorylation underlie each meiotic stage. We find that the phosphatase PP2A-B55 is reactivated at the Meiosis I/II transition resulting in the preferential dephosphorylation of threonine residues. Selective dephosphorylation is critical for directing the MI / MII transition as altering PP2A-B55 substrate preferences disrupts key cell cycle events after meiosis I. In addition, threonine to serine substitution of a conserved phosphorylation site in the substrate INCENP prevents its relocalization at anaphase I. Thus, through its inherent phospho-threonine preference, PP2A-B55 imposes specific phosphoregulated behaviors that distinguish the two meiotic divisions. |
HostingRepository | MassIVE |
AnnounceDate | 2021-08-12 |
AnnouncementXML | Submission_2021-08-12_13:05:56.135.xml |
DigitalObjectIdentifier | |
ReviewLevel | Non peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Mark Adamo |
SpeciesList | scientific name: Patiria miniata; common name: bat star; NCBI TaxID: 46514; |
ModificationList | TMT6plex; Carbamidomethyl; Oxidation; Phospho |
Instrument | Orbitrap Fusion; Orbitrap Fusion Lumos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
---|---|---|---|
0 | 2020-08-14 12:45:34 | ID requested | |
⏵ 1 | 2021-08-12 13:05:56 | announced |
Publication List
no publication |
Keyword List
submitter keyword: starfish, sea star, gamete, meiosis, oocyte, prophase, PP1, PP2A, PP2A-B55, protein phosphatase, phosphorylation, dephosphorylation, INCENP, TMT |
Contact List
Arminja Kettenbach | |
---|---|
contact affiliation | The Geisel School of Medicine at Dartmouth |
contact email | arminja.n.kettenbach@dartmouth.edu |
lab head | |
Mark Adamo | |
contact affiliation | Dartmouth College |
contact email | mark.e.adamo@dartmouth.edu |
dataset submitter |
Full Dataset Link List
MassIVE dataset URI |
Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://massive.ucsd.edu/MSV000085949/ |