Evidence map›Paper›PMID 29183978›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Proteomics of phosphorylation and protein dynamics during fertilization and meiotic exit in the

Marc Presler, Elizabeth Van Itallie, Allon M Klein, Ryan Kunz, Margaret L Coughlin, Leonid Peshkin, Steven P Gygi, Martin Wühr, Marc W Kirschner

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.6field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 57 citations in OpenAlex.

  1. Variable thresholds for phosphorylation targets of the ERK signaling pathway.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  10. The fitness cost of spurious phosphorylation.bioRxiv : the preprint server for biology · 2023
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  12. Review
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  19. Transcriptomics and Proteomics Methods forCold Spring Harbor protocols · 2020
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Marc PreslerDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115.
Elizabeth Van ItallieDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115.
Allon M KleinDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115.
Ryan KunzDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115.
Margaret L CoughlinDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115.
Leonid PeshkinDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115.
Steven P GygiDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115.
Martin WührDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115; wuhr@princeton.edu marc@hms.harvard.edu.
Marc W KirschnerDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115; wuhr@princeton.edu marc@hms.harvard.edu.
Harvard University · USCenter for Systems Biology · US

Funding

Systems Analysis of cell type differentiation in Xenopus developmentR01HD073104 · NICHD · HARVARD MEDICAL SCHOOL · PI KIRSCHNER, MARC WALLACE, PESHKIN, LEON · 2012 to 2022
$6.7M
MICROTUBULE DYNAMICS AND MITOTIC MECHANISMR01GM039565 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1988 to 2018
$6.2M
MICROTUBULE DYNAMICS AND MITOTIC MECHANISMR37GM039565 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1997 to 2006
$3.2M
Proteomics of Cell Signaling in Embryogenesis.R01HD091846 · NICHD · HARVARD MEDICAL SCHOOL · PI GYGI, STEVEN P, KIRSCHNER, MARC WALLACE · 2017 to 2021
$3.1M
Cell Cycle proteomicsin XenopusR01GM103785 · NIGMS · HARVARD MEDICAL SCHOOL · PI KIRSCHNER, MARC WALLACE · 2012 to 2016
$2.2M
NICHD NIH HHS R01 HD073104NICHD NIH HHS R01 HD091846NIGMS NIH HHS R01 GM039565NIGMS NIH HHS R01 GM103785NIGMS NIH HHS R37 GM039565
6 · The paper itself

Abstract

Fertilization releases the meiotic arrest and initiates the events that prepare the egg 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 phosphoregulation is still unknown. We examined absolute protein and phosphosite dynamics of the fertilization response by mass spectrometry-based proteomics in electroactivated eggs. To do this, we developed an approach for calculating the stoichiometry of phosphosites from multiplexed proteomics that is compatible with dynamic, stable, and multisite phosphorylation. Overall, the data suggest that degradation is limited to a few low-abundance proteins. However, this degradation 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 and components of the slow block to polyspermy. The analytical approaches demonstrated here are broadly applicable to studies of dynamic biological systems.

Indexed as

AnimalsCalciumFemaleFertilizationMeiosisNuclear Pore Complex ProteinsOvumPhosphorylationProtein Processing, Post-TranslationalProteolysisProteomeXenopus laevisCalciumNuclear Pore Complex ProteinsProteomecell cycleconfidence intervalspolyspermy blockstoichiometryTMT

Identifiers

PMID29183978
PMCPMC5740657
OpenAlexW2949607482

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.