Evidence map›Paper›PMID 26259730›Full record

ArticleCell calcium2015

Effect of M-phase kinase phosphorylations on type 1 inositol 1,4,5-trisphosphate receptor-mediated Ca2+ responses in mouse eggs.

Nan Zhang, Sook Young Yoon, Jan B Parys, Rafael A Fissore

Open access · greenAbstract read
In one paragraph

Article in Cell calcium, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. CaCold Spring Harbor perspectives in biology · 2019
    Review
  6. Article
  7. Review
  8. Ion Channel Function During Oocyte Maturation and Fertilization.Frontiers in cell and developmental biology · 2018
    Review
  9. Review
  10. Review
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

4 authors at 4 institutions in 3 countries.

Nan ZhangDepartment of Veterinary and Animal Sciences, University of Massachusetts, Amherst, MA 01003, USA; Department of Obstetrics and Gynecology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Sook Young YoonFertility Center of CHA Gangnam Medical Center, College of Medicine, CHA University, Seoul 135-081, Republic of Korea.
Jan B ParysKU Leuven, Laboratory of Molecular and Cellular Signaling, Department of Cellular and Molecular Medicine, Campus Gasthuisberg O/N-I box 802, Herestraat 49, BE-3000 Leuven, Belgium.
Rafael A FissoreDepartment of Veterinary and Animal Sciences, University of Massachusetts, Amherst, MA 01003, USA. Electronic address: rfissore@vasci.umass.edu.
CHA University · KRKU Leuven · BENorthwestern University · USUniversity of Massachusetts Amherst · US

Funding

LP3R-1 Regulation and Egg ActivationR01HD051872 · NICHD · UNIVERSITY OF MASSACHUSETTS AMHERST · PI FISSORE, RAFAEL ANTONIO · 2007 to 2011
$1.3M
NICHD NIH HHS R01 HD051872
6 · The paper itself

Abstract

The type 1 inositol 1,4,5-trisphosphate receptor (IP3R1) mediates increases in the intracellular concentration of Ca(2+) ([Ca(2+)]i) during fertilization in mammalian eggs. The activity of IP3R1 is enhanced during oocyte maturation, and phosphorylations by M-phase kinases are thought to positively regulate the activity of IP3R1. Accordingly, we and others have found that IP3R1 is phosphorylated at S(421), T(799) (by Cdk1) and at S(436) (by ERK). Nevertheless, the effects of these phosphorylations on the function of the receptor and their impact on [Ca(2+)]i oscillations in eggs have not been clearly examined. To address this, we expressed in mouse oocytes an IP3R1 variant with the three indicated phosphorylation sites replaced by acidic residues, IIIE-IP3R1, such that it would act like a constitutively phosphorylated IP3R1, and examined [Ca(2+)]i parameters in response to stimuli. We found that overexpression of wild type (wt-IP3R1) or IIIE-IP3R1 in oocytes containing endogenous receptors caused dominant negative-like effects on Ca(2+) release and oscillations. Therefore, we first selectively removed the endogenous IP3R1, and subsequently expressed the exogenous receptors. We found that in response to injection of PLCζ cRNA, eggs without endogenous IP3R1 failed to mount persistent Ca(2+) oscillations, although expression of wt-IP3R1 restored their [Ca(2+)]i oscillatory activity. We also observed that the Ca(2+) oscillatory ability and the sensitivity to IP3 in eggs expressing IIIE-IP3R1 were greater than in those expressing wt-IP3R1. Lastly, we found that exogenous IP3R1s are resistant to downregulation and support longer oscillations and of higher amplitude. Altogether, our results show that phosphorylations by Cdk1 and MAPK enhance the activity of IP3R1, which is consistent with its maximal activity observed at the time of fertilization and the role of Ca(2+) release in egg activation.

Indexed as

Calcium SignalingCell DivisionAnimalsCalciumFemaleInositol 1,4,5-Trisphosphate ReceptorsMiceOocytesPhosphorylationCalciumInositol 1,4,5-Trisphosphate ReceptorsCalciumEgg activationIP3R1Mouse eggs

Identifiers

PMID26259730
PMCPMC4631651
OpenAlexW2194279174

What OpenQuestion holds

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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.