PXD006639

PXD006639 is an original dataset announced via ProteomeXchange.

Title	Proteomics of phosphorylation and protein dynamics during fertilization and meiotic exit in the Xenopus egg
Description	Fertilization triggers release from meiotic arrest and initiates events that prepare for the ensuing developmental program. Protein degradation and phosphorylation are known to regulate protein activity during this process. However, the full extent of protein loss and phospho-regulation is still unknown. We examined absolute protein and phospho-site dynamics after fertilization by mass spectrometry-based proteomics. To do this, we developed a new approach for calculating the stoichiometry of phospho-sites from multiplexed proteomics compatible with dynamic, stable and multi-site phosphorylation. Overall, the data suggest that degradation is limited to a few low abundance proteins. However, this degradation in part promotes extensive dephosphorylation that occurs over a wide range of abundances during meiotic exit. We also show that eggs release a large amount of protein into the medium just after fertilization, most likely related to the blocks to polyspermy. Concomitantly, there is a substantial increase in phosphorylation likely tied to calcium activated kinases. We identify putative degradation targets as well as new components of the block to polyspermy. The analytical approaches demonstrated here are broadly applicable to studies of dynamic biological systems.
HostingRepository	PRIDE
AnnounceDate	2017-11-29
AnnouncementXML	Submission_2017-12-11_03:57:27.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Marc Presler
SpeciesList	scientific name: Xenopus laevis (African clawed frog); NCBI TaxID: 8355;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; phosphorylated residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2017-06-01 00:45:13	ID requested
1	2017-11-29 03:02:58	announced
⏵ 2	2017-12-11 03:57:28	announced	Updated publication reference for PubMed record(s): 29183978.

Presler M, Van Itallie E, Klein AM, Kunz R, Coughlin ML, Peshkin L, Gygi SP, W, ü, hr M, Kirschner MW, egg. Proc Natl Acad Sci U S A, 114(50):E10838-E10847(2017) [pubmed]

curator keyword: Biological

submitter keyword: Xenopus, egg, fertilization,

Marc W. Kirschner
contact affiliation	Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA
contact email	marc@hms.harvard.edu
lab head
Marc Presler
contact affiliation	Graduate Student
contact email	marcpresler@fas.harvard.edu
dataset submitter

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://ftp.pride.ebi.ac.uk/pride/data/archive/2017/11/PXD006639

PRIDE project URI

• PRIDE
  1. PXD006639
     1. Label: PRIDE project
     2. Name: Proteomics of phosphorylation and protein dynamics during fertilization and meiotic exit in the Xenopus egg