Evidence map›Paper›PMID 17047254›Full record

ArticleMolecular and cellular biology2006

ZP2 and ZP3 traffic independently within oocytes prior to assembly into the extracellular zona pellucida.

Tanya Hoodbhoy, Manuel Avilés, Boris Baibakov, Olga Epifano, María Jiménez-Movilla, Lyn Gauthier, Jurrien Dean

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Germ Granules in Animal Oogenesis.Journal of developmental biology · 2022
    Review
  7. Review
  8. New Insights into the Mammalian Egg Zona Pellucida.International journal of molecular sciences · 2021
    Review
  9. Article
  10. Mammalian egg coat modifications and the block to polyspermy.Molecular reproduction and development · 2020
    Review
  11. Article
  12. Article
  13. ZP2 pathogenic variants cause in vitro fertilization failure and female infertility.Genetics in medicine : official journal of the American College of Medical Genetics · 2019
    Article
  14. Article
  15. Article
  16. Mutant ZP1 in familial infertility.The New England journal of medicine · 2014
    Article
  17. Review
  18. Article
  19. Article
  20. 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

7 authors at 3 institutions in 2 countries.

Tanya HoodbhoyLaboratory of Cellular and Developmental Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892-8028, USA.
Manuel Avilés
Boris Baibakov
Olga Epifano
María Jiménez-Movilla
Lyn Gauthier
Jurrien Dean
National Institutes of Health · USNational Institute of Diabetes and Digestive and Kidney Diseases · USUniversidad de Murcia · ES

Funding

Molecular Biology of the OocyteZIADK015603 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI DEAN, JURRIEN · 2009 to 2025
$43.2M
Molecular Biology of the Zona PellucidaZ01DK015603 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI DEAN, JURRIEN · 2007 to 2008
$971k
MAMMALIAN GONADOGENESIS, FOLLICULOGENESIS AND FERTILIZATIONZ01DK015506 · NIDDK · DIABETES, DIGESTIVE, KIDNEY DISEASES · PI DEAN, JURRIEN · 1986 to 2006
–
Intramural NIH HHS
6 · The paper itself

Abstract

The extracellular zona pellucida surrounds mammalian eggs and mediates taxon-specific sperm-egg recognition at fertilization. In mice, the zona pellucida is composed of three glycoproteins, but the presence of ZP2 and ZP3 is sufficient to form a biologically functional structure. Each zona pellucida glycoprotein is synthesized in growing oocytes and traffics through the endomembrane system to the cell surface, where it is released from a transmembrane domain and assembled into the insoluble zona pellucida matrix. ZP2 and ZP3 colocalize in the endoplasmic reticulum and in 1- to 5-microm post-Golgi structures comprising multivesicular aggregates (MVA), but a coimmunoprecipitation assay does not detect physical interactions. In addition, ZP2 traffics normally in growing oocytes in the absence of ZP3 or if ZP3 has been mutated to prevent incorporation into the zona pellucida matrix, complementing earlier studies indicating the independence of ZP3 secretion in Zp2 null mice. N glycosylation has been implicated in correct protein folding and intracellular trafficking of secreted proteins. Although ZP3 contain five N-glycans, enhanced green fluorescent protein-tagged ZP3 lacking N glycosylation sites is present in MVA and is incorporated into the zona pellucida matrix of transgenic mice. Thus, ZP2 secretion is seemingly unaffected by ZP3 lacking N-glycans. Taken together, these observations indicate that ZP2 and ZP3 traffic independently through the oocyte prior to assembly into the zona pellucida.

Indexed as

AnimalsEgg ProteinsEndoplasmic ReticulumFemaleFluorescent DyesMembrane GlycoproteinsMiceMice, KnockoutMice, TransgenicOocytesPolysaccharidesReceptors, Cell SurfaceRecombinant Fusion ProteinsZona PellucidaZona Pellucida GlycoproteinsEgg ProteinsFluorescent DyesMembrane GlycoproteinsPolysaccharidesReceptors, Cell SurfaceRecombinant Fusion ProteinsZona Pellucida GlycoproteinsZp2 protein, mouseZp3 protein, mouse

Identifiers

PMID17047254
PMCPMC1636726
OpenAlexW2101202769

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.