Evidence map›Paper›PMID 31672133›Full record

ArticleBMC biology2019

GLIPR1L1 is an IZUMO-binding protein required for optimal fertilization in the mouse.

Avinash S Gaikwad, Amanda L Anderson, D Jo Merriner, Anne E O'Connor, Brendan J Houston, R John Aitken, Moira K O'Bryan, Brett Nixon

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 1 synthesis or guideline pooled it, 30 citations in OpenAlex.

  1. Pooled it
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  12. Update on Novel Hormonal and Nonhormonal Male Contraceptive Development.The Journal of clinical endocrinology and metabolism · 2021
    Review
  13. CRISPs Function to Boost Sperm Power Output and Motility.Frontiers in cell and developmental biology · 2021
    Article
  14. Article
  15. Bio-protocol · 2020
    Article
  16. Article
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

8 authors at 2 institutions in 1 country.

Avinash S GaikwadThe School of Biological Sciences, Monash University, Melbourne, VIC, 3800, Australia.
Amanda L AndersonPriority Research Centre for Reproductive Science, School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW, 2308, Australia.
D Jo MerrinerThe School of Biological Sciences, Monash University, Melbourne, VIC, 3800, Australia.
Anne E O'ConnorThe School of Biological Sciences, Monash University, Melbourne, VIC, 3800, Australia.
Brendan J HoustonThe School of Biological Sciences, Monash University, Melbourne, VIC, 3800, Australia.
R John AitkenPriority Research Centre for Reproductive Science, School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW, 2308, Australia.
Moira K O'BryanThe School of Biological Sciences, Monash University, Melbourne, VIC, 3800, Australia. moira.obryan@monash.edu.
Brett NixonPriority Research Centre for Reproductive Science, School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW, 2308, Australia. Brett.Nixon@newcastle.edu.au.ORCID 0000-0003-2745-8188
Monash University · AUUniversity of Newcastle Australia · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe sperm protein IZUMO1 (Izumo sperm-egg fusion 1) and its recently identified binding partner on the oolemma, IZUMO1R, are among the first ligand-receptor pairs shown to be essential for gamete recognition and adhesion. However, the IZUMO1-IZUMO1R interaction does not appear to be directly responsible for promoting the fusion of the gamete membranes, suggesting that this critical phase of the fertilization cascade requires the concerted action of alternative fusogenic machinery. It has therefore been proposed that IZUMO1 may play a secondary role in the organization and/or stabilization of higher-order heteromeric complexes in spermatozoa that are required for membrane fusion.

resultsHere, we show that fertilization-competent (acrosome reacted) mouse spermatozoa harbor several high molecular weight protein complexes, a subset of which are readily able to adhere to solubilized oolemmal proteins. At least two of these complexes contain IZUMO1 in partnership with GLI pathogenesis-related 1 like 1 (GLIPR1L1). This interaction is associated with lipid rafts and is dynamically remodeled upon the induction of acrosomal exocytosis in preparation for sperm adhesion to the oolemma. Accordingly, the selective ablation of GLIPR1L1 leads to compromised sperm function characterized by a reduced ability to undergo the acrosome reaction and a failure of IZUMO1 redistribution.

conclusionsCollectively, this study characterizes multimeric protein complexes on the sperm surface and identifies GLIPRL1L1 as a physiologically relevant regulator of IZUMO1 function and the fertilization process.

Indexed as

AnimalsFertilizationGlycoproteinsImmunoglobulinsMaleMembrane ProteinsMiceSpermatozoaGlipr1l1 protein, mouseGlycoproteinsImmunoglobulinsIzumo1 protein, mouseMembrane ProteinsCapacitationFertilizationGLIPR1L1IZUMOMale fertilityMale infertilityOolemmaSpermatozoa

Identifiers

PMID31672133
PMCPMC6824042
OpenAlexW2982369665

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.