ArticleMolecular reproduction and development2009
Izumo is part of a multiprotein family whose members form large complexes on mammalian sperm.
Article in Molecular reproduction and development, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers, 1 of them a synthesis that pooled it.
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Who cites it
63 citing papers in PubMed, 1 synthesis or guideline pooled it, 139 citations in OpenAlex.
- The Role of Sperm Proteins IZUMO1 and TMEM95 in Mammalian Fertilization: A Systematic Review.International journal of molecular sciences · 2022Pooled it
- Sperm surface protein disulfide isomerase ERp57 is crucial for mammalian fertilization but functions independently of IZUMO1.Cellular & molecular biology letters · 2026Article
- Article
- JUNO-coated beads as a functional assay to capture and characterize fertilization-competent human sperm.Human reproduction open · 2026Article
- Membrane Fusions During Mammalian Fertilization.Advances in experimental medicine and biology · 2026Review
- TheBiomolecules · 2025Review
- Spermatozoa lacking TEX51 display hypofertility and defects in morphology.Communications biology · 2025Article
- Exploring the impact of lipid stress on sperm cytoskeleton: insights and prospects.Nature reviews. Urology · 2025Review
- Allosteric inhibition of the IZUMO1-JUNO fertilization complex by the naturally occurring antisperm antibody OBF13.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Implication of IZUMO2 in the cell-in-cell phenomenon: A potential therapeutic target for triple-negative breast cancer.Thoracic cancer · 2024Article
- New insights into posttranslational modifications of proteins during bull sperm capacitation.Cell communication and signaling : CCS · 2023Article
- Testis-specific actin-like 7A (ACTL7A) is an indispensable protein for subacrosomal-associated F-actin formation, acrosomal anchoring, and male fertility.Molecular human reproduction · 2023Article
- 1700029I15Rik orchestrates the biosynthesis of acrosomal membrane proteins required for sperm-egg interaction.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A novel function for the sperm adhesion protein IZUMO1 in cell-cell fusion.The Journal of cell biology · 2023Article
- Immunogenicity and contraceptive efficacy of plant-produced putative mouse-specific contraceptive peptides.Frontiers in plant science · 2023Article
- The fate of porcine sperm CRISP2 from the perinuclear theca before and after in vitro fertilization†.Biology of reproduction · 2022Article
- SPACA6 ectodomain structure reveals a conserved superfamily of gamete fusion-associated proteins.Communications biology · 2022Article
- C11orf94/Frey is a key regulator for male fertility by controlling Izumo1 complex assembly.Science advances · 2022Article
- Strategies for successful designing of immunocontraceptive vaccines and recent updates in vaccine development against sexually transmitted infections - A review.Saudi journal of biological sciences · 2022Review
3 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Izumo, a sperm membrane protein, is essential for gamete fusion in the mouse. It has an Immunoglobulin (Ig) domain and an N-terminal domain for which neither the functions nor homologous sequences are known. In the present work we identified three novel proteins showing an N-terminal domain with significant homology to the N-terminal domain of Izumo. We named this region "Izumo domain," and the novel proteins "Izumo 2," "Izumo 3," and "Izumo 4," retaining "Izumo 1" for the first described member of the family. Izumo 1-3 are transmembrane proteins expressed specifically in the testis, and Izumo 4 is a soluble protein expressed in the testis and in other tissues. Electrophoresis under mildly denaturing conditions, followed by Western blot analysis, showed that Izumo 1, 3, and 4 formed protein complexes on sperm, Izumo 1 forming several larger complexes and Izumo 3 and 4 forming a single larger complex. Studies using different recombinant Izumo constructs suggested the Izumo domain possesses the ability to form dimers, whereas the transmembrane domain or the cytoplasmic domain or both of Izumo 1 are required for the formation of multimers of higher order. Co-immunoprecipitation studies showed the presence of other sperm proteins associated with Izumo 1, suggesting Izumo 1 forms a multiprotein membrane complex. Our results raise the possibility that Izumo 1 might be involved in organizing or stabilizing a multiprotein complex essential for the function of the membrane fusion machinery.
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