Izumo is part of a multiprotein family whose members form large complexes on mammalian sperm
Open accessAbstract
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. Mol. Reprod. Dev. 76: 1188–1199, 2009. © 2009 Wiley‐Liss, Inc.
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A splice site change in IZUMO4 is a possible SNC that might be relevant, since proteins encoded by the IZUMO family form complexes on mammalian sperm.
“Another possible SNC that might be relevant in this context is a splice site change in IZUMO4, since proteins encoded by the IZUMO family form complexes on mammalian sperm175.”
From A catalog of single nucleotide changes distinguishing modern humans from archaic hominins (2019) · cites this paper as [175]
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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302 · see citing works
Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetii
Voth, D. E., & Heinzen, R. A. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.00901.x · Cited by 11,773 · see citing works
Membrane Fusion: Grappling with SNARE and SM Proteins
Südhof, T. C., & Rothman, J. E. (2009) · Science · doi:10.1126/science.1161748 · Cited by 2,027 · see citing works
The rapid evolution of reproductive proteins
Swanson, W. J., & Vacquier, V. D. (2002) · Nature Reviews Genetics · doi:10.1038/nrg733 · Cited by 1,316 · see citing works
The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs
Inoue, N., Ikawa, M., Isotani, A., & Okabe, M. (2005) · Nature · doi:10.1038/nature03362 · Cited by 832 · see citing works
Requirement of CD9 on the Egg Plasma Membrane for Fertilization
Miyado, K., Yamada, G., Yamada, S., Hasuwa, H., Nakamura, Y., Ryu, F., Suzuki, K., Kosai, K.-I., Inoue, K., Ogura, A., et al. (2000) · Science · doi:10.1126/science.287.5451.321 · Cited by 686 · see citing works
Severely Reduced Female Fertility in CD9-Deficient Mice
Naour, F. L., Rubinstein, E., Jasmin, C., Prenant, M., & Boucheix, C. (2000) · Science · doi:10.1126/science.287.5451.319 · Cited by 645 · see citing works
Rizo, J., & Rosenmund, C. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1450 · Cited by 538 · see citing works
The gamete fusion process is defective in eggs of Cd9-deficient mice
Kaji, K., Oda, S., Shikano, T., Ohnuki, T., Uematsu, Y., Sakagami, J., Tada, N., Miyazaki, S., & Kudō, A. (2000) · Nature Genetics · doi:10.1038/73502 · Cited by 490 · see citing works
The CRAC channel consists of a tetramer formed by Stim-induced dimerization of Orai dimers
Penna, A., Demuro, A., Yeromin, A. V., Zhang, S. L., Safrina, O., Parker, I., & Cahalan, M. D. (2008) · Nature · doi:10.1038/nature07338 · Cited by 384 · see citing works
PROMALS: towards accurate multiple sequence alignments of distantly related proteins
Pei, J., & Grishin, N. V. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm017 · Cited by 339 · see citing works
Self-citationLiu, Y., Tewari, R., Ning, J., Blagborough, A. M., Garbom, S., Pei, J., Grishin, N. V., Steele, R. E., Sinden, R. E., Snell, W. J., et al. (2008) · Genes & Development · doi:10.1101/gad.1656508 · Cited by 323 · see citing works
Self-citationAnalysis of Loss of Adhesive Function in Sperm Lacking Cyritestin or Fertilin β
Nishimura, H., Cho, C., Branciforte, D., Myles, D. G., & Primakoff, P. (2001) · Developmental Biology · doi:10.1006/dbio.2001.0166 · Cited by 255 · see citing works
Self-citationAtanasiu, D., Whitbeck, J. C., Cairns, T. M., Reilly, B., Cohen, G. H., & Eisenberg, R. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707452104 · Cited by 183 · see citing works
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Carlson, A. E., Quill, T. A., Westenbroek, R. E., Schuh-Huerta, S. M., Hille, B., & Babcock, D. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501430200 · Cited by 177 · see citing works
The molecular players of sperm–egg fusion in mammals
Rubinstein, E., Ziyyat, A., Wolf, J., Naour, F. L., & Boucheix, C. (2006) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2006.02.012 · Cited by 164 · see citing works
Sleight, S. B., Miranda, P. V., Plaskett, N.-W., Maier, B., Lysiak, J. J., Scrable, H. J., Herr, J. C., & Visconti, P. E. (2005) · Biology of Reproduction · doi:10.1095/biolreprod.105.041533 · Cited by 154 · see citing works
The multipartite system that mediates entry of herpes simplex virus into the cell
Campadelli‐Fiume, G., Amasio, M., Avitabile, E., Cerretani, A., Forghieri, C., Gianni, T., & Menotti, L. (2007) · Reviews in Medical Virology · doi:10.1002/rmv.546 · Cited by 152 · see citing works
Novel method for evaluation of the oligomeric structure of membrane proteins
Ramjeesingh, M., Huan, L., Garami, E., & Bear, C. E. (1999) · Biochemical Journal · doi:10.1042/bj3420119 · Cited by 136 · see citing works
Proteomic analysis of sperm regions that mediate sperm‐egg interactions
Stein, K. K., Go, J. C., Lane, W. S., Primakoff, P., & Myles, D. G. (2006) · PROTEOMICS · doi:10.1002/pmic.200500845 · Cited by 116 · see citing works
Self-citationAvitabile, E., Forghieri, C., & Campadelli‐Fiume, G. (2007) · Journal of Virology · doi:10.1128/jvi.01343-07 · Cited by 109 · see citing works
Comparative Analysis of Testis Protein Evolution in Rodents
Turner, L. M., Chuong, E. B., & Hoekstra, H. E. (2008) · Genetics · doi:10.1534/genetics.107.085902 · Cited by 79 · see citing works
Miranda, P. V., Allaire, A., Sosnik, J., & Visconti, P. E. (2009) · Biology of Reproduction · doi:10.1095/biolreprod.108.075242 · Cited by 74 · see citing works
Direct Binding of the Ligand PSG17 to CD9 Requires a CD9 Site Essential for Sperm-Egg Fusion
Ellerman, D. A., Ha, C. T., Primakoff, P., Myles, D. G., & Dveksler, G. S. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-04-0244 · Cited by 73 · see citing works
Self-citationPutative sperm fusion protein IZUMO and the role of N-glycosylation
Inoue, N., Ikawa, M., & Okabe, M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.10.073 · Cited by 68 · see citing works
Nishimura, H., Myles, D. G., & Primakoff, P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702268200 · Cited by 61 · see citing works
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Sendler, E. D., Johnson, G. D., Mao, S., Goodrich, R. J., Diamond, M. P., Hauser, R. B., & Krawetz, S. A. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt132 · Cited by 326 · see citing works
Florman, H. M., & Fissore, R. A. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397175-3.00004-1 · Cited by 199 · see citing works
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Aydin, H., Sultana, A., Li, S., Thavalingam, A., & Lee, J. E. (2016) · Nature · doi:10.1038/nature18595 · Cited by 179 · see citing works
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Ohto, U., Ishida, H., Krayukhina, E., Uchiyama, S., Inoue, N., & Shimizu, T. (2016) · Nature · doi:10.1038/nature18596 · Cited by 155 · see citing works
Molecular dissection of IZUMO1, a sperm protein essential for sperm-egg fusion
Inoue, N., Hamada, D., Kamikubo, H., Hirata, K., Kataoka, M., Yamamoto, M., Ikawa, M., Okabe, M., & Hagihara, Y. (2013) · Development · doi:10.1242/dev.094854 · Cited by 127 · see citing works
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Oocyte-triggered dimerization of sperm IZUMO1 promotes sperm–egg fusion in mice
Inoue, N., Hagihara, Y., Wright, D., Suzuki, T., & Wada, I. (2015) · Nature Communications · doi:10.1038/ncomms9858 · Cited by 110 · see citing works
A catalog of single nucleotide changes distinguishing modern humans from archaic hominins
Kuhlwilm, M., & Boeckx, C. (2019) · Scientific Reports · doi:10.1038/s41598-019-44877-x · Cited by 108 · see citing works
Vickram, A. S., Dhama, K., Chakraborty, S., Samad, H. A., Latheef, S. K., Sharun, K., Khurana, S. K., Archana, K., Tiwari, R., Bhatt, P., et al. (2019) · Vaccines · doi:10.3390/vaccines7030116 · Cited by 103 · see citing works
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Evans, J. P. (2011) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020911-153339 · Cited by 92 · see citing works
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Findlay, G. D., & Swanson, W. J. (2009) · BioEssays · doi:10.1002/bies.200900127 · Cited by 89 · see citing works
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Bianchi, E., & Wright, G. J. (2016) · Annual Review of Genetics · doi:10.1146/annurev-genet-121415-121834 · Cited by 88 · see citing works
Chalbi, M., Barraud‐Lange, V., Ravaux, B., Howan, K., Rodríguez, N., Soule, P., Ndzoudi, A., Boucheix, C., Rubinstein, E., Wolf, J. P., et al. (2014) · Development · doi:10.1242/dev.111534 · Cited by 87 · see citing works
The molecular mechanisms mediating mammalian fertilization
Bhakta, H., Refai, F. H., & Avella, M. (2019) · Development · doi:10.1242/dev.176966 · Cited by 83 · see citing works
Membrane Fusions During Mammalian Fertilization
Gadella, B. M., & Evans, J. P. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-0763-4_5 · Cited by 79 · see citing works
A conserved fertilization complex bridges sperm and egg in vertebrates
Deneke, V. E., Blaha, A., Lu, Y., Suwita, J. P., Draper, J. M., Phan, C. S., Panser, K., Schleiffer, A., Jacob, L., Humer, T., et al. (2024) · Cell · doi:10.1016/j.cell.2024.09.035 · Cited by 78 · see citing works
The cell biology of fertilization: Gamete attachment and fusion
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The mechanism of sperm–egg interaction and the involvement of IZUMO1 in fusion
Inoue, N., Ikawa, M., & Okabe, M. (2010) · Asian Journal of Andrology · doi:10.1038/aja.2010.70 · Cited by 72 · see citing works
Sperm-Egg Fusion: A Molecular Enigma of Mammalian Reproduction
Klinovská, K., Šebková, N., & Komrsková, K. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150610652 · Cited by 68 · see citing works
Anifandis, G., Messini, C. I., Dafopoulos, K. C., Sotiriou, S., & Messinis, I. E. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150712972 · Cited by 64 · see citing works
Izumo1 and Juno: the evolutionary origins and coevolution of essential sperm–egg binding partners
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Zhou, X., & Platt, J. L. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-0763-4_4 · Cited by 59 · see citing works
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Dorus, S., Skerget, S., & Karr, T. L. (2012) · Systems Biology in Reproductive Medicine · doi:10.3109/19396368.2012.700442 · Cited by 54 · see citing works
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Bromfield, E. G., & Nixon, B. (2012) · Reproduction · doi:10.1530/rep-12-0316 · Cited by 46 · see citing works
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Kasvandik, S., Sillaste, G., Velthut‐Meikas, A., Mikelsaar, A., Hallap, T., Padrik, P., Tenson, T., Jaakma, Ü., Kõks, S., & Salumets, A. (2015) · PROTEOMICS · doi:10.1002/pmic.201400297 · Cited by 44 · see citing works
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Brukman, N. G., Nakajima, K. P., Valansi, C., Flyak, K., Li, X., Higashiyama, T., & Podbilewicz, B. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202207147 · Cited by 43 · see citing works
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Mostek, A., Janta, A., Majewska, A. M., & Ciereszko, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22157903 · Cited by 42 · see citing works
Liu, Y., Pei, J., Grishin, N. V., & Snell, W. J. (2015) · Development · doi:10.1242/dev.118844 · Cited by 40 · see citing works
Self-citationNew Insights into the Molecular Events of Mammalian Fertilization
Satouh, Y., & Ikawa, M. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.08.006 · Cited by 40 · see citing works
Kumar, P., Wang, M., Isachenko, E., Rahimi, G., Mallmann, P. K., Wang, W., von Brandenstein, M., & Isachenko, V. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.672862 · Cited by 40 · see citing works
Protein biomarkers for male artificial insemination subfertility in bovine spermatozoa
Harayama, H., Minami, K., Kishida, K., & Noda, T. (2017) · Reproductive Medicine and Biology · doi:10.1002/rmb2.12021 · Cited by 39 · see citing works
Fernández-Fuertes, B., Laguna‐Barraza, R., Fernández‐González, R., Gutiérrez‐Adán, A., Blanco, A., O’Doherty, A., Fenza, M. D., Kelly, A. K., Kölle, S., & Lonergan, P. (2017) · Biology of Reproduction · doi:10.1093/biolre/iox065 · Cited by 39 · see citing works
The molecular complexity of fertilization: Introducing the concept of a fertilization synapse
Krauchunas, A. R., Marcello, M. R., & Singson, A. W. (2016) · Molecular Reproduction and Development · doi:10.1002/mrd.22634 · Cited by 39 · see citing works
Cell Fusion in Health and Disease
Dittmar, T., & Zänker, K. S. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-0763-4 · Cited by 39 · see citing works
Fertilization and the oocyte-to-embryo transition in C. elegans
Marcello, M. R., & Singson, A. W. (2010) · BMB Reports · doi:10.3858/bmbrep.2010.43.6.389 · Cited by 37 · see citing works
Evolution of programmed cell fusion: Common mechanisms and distinct functions
Oren‐Suissa, M., & Podbilewicz, B. (2010) · Developmental Dynamics · doi:10.1002/dvdy.22284 · Cited by 35 · see citing works
Nishimura, H., Tajima, T., Comstra, H. S., Gleason, E. J., & L’Hernault, S. W. (2015) · Current Biology · doi:10.1016/j.cub.2015.10.056 · Cited by 34 · see citing works
Engineering monoclonal antibody-based contraception and multipurpose prevention technologies†
Anderson, D. J., Politch, J. A., Cone, R. A., Zeitlin, L., Lai, S. K., Santangelo, P. J., Moench, T. R., & Whaley, K. J. (2020) · Biology of Reproduction · doi:10.1093/biolre/ioaa096 · Cited by 33 · see citing works
Presence and Incidence of Izumo Antibodies in Sera of Immunoinfertile Women and Men
Clark, S., & Naz, R. K. (2012) · American Journal of Reproductive Immunology · doi:10.1111/aji.12060 · Cited by 32 · see citing works
Changes of IZUMO1 in bull spermatozoa during the maturation, acrosome reaction, and cryopreservation
Fukuda, M., Sakase, M., Fukushima, M., & Harayama, H. (2016) · Theriogenology · doi:10.1016/j.theriogenology.2016.07.010 · Cited by 31 · see citing works
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Gaikwad, A., Anderson, A. L., Merriner, D. J., O’Connor, A. E., Houston, B. J., Aitken, R. J., O’Bryan, M. K., & Nixon, B. (2019) · BMC Biology · doi:10.1186/s12915-019-0701-1 · Cited by 30 · see citing works
Deep learning insights into the architecture of the mammalian egg-sperm fusion synapse
Elofsson, A., Han, L., Bianchi, E., Wright, G. J., & Jovine, L. (2024) · eLife · doi:10.7554/elife.93131 · Cited by 36 · see citing works
New Insights into the Mechanisms and Roles of Cell–Cell Fusion
Shinn-Thomas, J. H., & Mohler, W. A. (2011) · International review of cytology · doi:10.1016/b978-0-12-386039-2.00005-5 · Cited by 29 · see citing works
Positive Selection and the Evolution ofizumoGenes in Mammals
Grayson, P., & Civetta, A. (2012) · International Journal of Evolutionary Biology · doi:10.1155/2012/958164 · Cited by 29 · see citing works
Nimlamool, W., Bean, B. S., & Lowe‐Krentz, L. J. (2013) · Molecular Reproduction and Development · doi:10.1002/mrd.22189 · Cited by 28 · see citing works
Wassarman, P. M. (2014) · Nature · doi:10.1038/nature13227 · Cited by 26 · see citing works
Equine seminal plasma and sperm membrane: Functional proteomic assessment
Guasti, P. N., de Souza, F. F., Scott, C., Papa, P. M., de Camargo, L. S., Schmith, R. A., Monteiro, G. A., Hartwig, F. P., & Papa, F. (2020) · Theriogenology · doi:10.1016/j.theriogenology.2020.06.014 · Cited by 28 · see citing works
Ferrer, P., Upadhyay, S., Ikawa, M., & Clement, T. M. (2023) · Molecular Human Reproduction · doi:10.1093/molehr/gaad005 · Cited by 26 · see citing works
Marcello, M. R., & Evans, J. P. (2010) · Molecular Human Reproduction · doi:10.1093/molehr/gaq029 · Cited by 26 · see citing works
Vicens, A., & Roldán, E. R. S. (2014) · Biology of Reproduction · doi:10.1095/biolreprod.113.116871 · Cited by 25 · see citing works
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Lu, Y., Shimada, K., Tang, S., Zhang, J., Ogawa, Y., Noda, T., Shibuya, H., & Ikawa, M. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2207263120 · Cited by 24 · see citing works
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Muro, Y., & Okabe, M. (2011) · Journal of Andrology · doi:10.2164/jandrol.110.010900 · Cited by 23 · see citing works
Leclerc, P., Goupil, S., Rioux, J., Lavoie‐Ouellet, C., Clark, M., Ruiz, J., & Saindon, A. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29421 · Cited by 23 · see citing works
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Vance, T. D. R., Yip, P., Jiménez, E., Li, S., Gawol, D., Byrnes, J., Usón, I., Ziyyat, A., & Lee, J. E. (2022) · Communications Biology · doi:10.1038/s42003-022-03883-y · Cited by 23 · see citing works
Molecular Cloning, Characterization of Porcine IZUMO1, an IgSF Family Member
Kim, E., Kim, J., Lee, Y., Song, B., Sim, B., Kim, S., Saitoh, T., Yazawa, H., Nunoya, T., & Chang, K. (2012) · Reproduction in Domestic Animals · doi:10.1111/j.1439-0531.2012.02037.x · Cited by 22 · see citing works
The Role of Sperm Proteins IZUMO1 and TMEM95 in Mammalian Fertilization: A Systematic Review
Hernández-Falcó, M., Sáez‐Espinosa, P., López-Botella, A., Aizpurúa, J., & Gómez‐Torres, M. J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073929 · Cited by 21 · see citing works
Nagdas, S. K., Smith, L., Medina-Ortiz, I., Hernandez-Encarnacion, L., & RAYCHOUDHURY, S. S. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2668-3 · Cited by 20 · see citing works
New insights into posttranslational modifications of proteins during bull sperm capacitation
Mostek, A., Majewska, A. M., Janta, A., & Ciereszko, A. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01080-w · Cited by 19 · see citing works
The enigmatic sperm proteins in mammalian fertilization: an overview†
Gahlay, G. K., & Rajput, N. (2020) · Biology of Reproduction · doi:10.1093/biolre/ioaa140 · Cited by 18 · see citing works
Rivera, A., & Swanson, W. J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.827454 · Cited by 18 · see citing works
Phopin, K., Nimlamool, W., Bartlett, M. J., & Bean, B. S. (2011) · Molecular Reproduction and Development · doi:10.1002/mrd.22016 · Cited by 18 · see citing works
Young, S. A. M., Miyata, H., Satouh, Y., Muto, M., Larsen, M. R., Aitken, R. J., Baker, M. A., & Ikawa, M. (2016) · Reproduction · doi:10.1530/rep-16-0150 · Cited by 16 · see citing works
IZUMO family member 3, IZUMO3, is involved in male fertility through the acrosome formation
Inoue, N., Satouh, Y., & Wada, I. (2021) · Molecular Reproduction and Development · doi:10.1002/mrd.23520 · Cited by 15 · see citing works
Phosphorylation of Izumo1 and Its Role in Male Infertility
Baker, M., Young, S. A. M., & Aitken, R. J. (2015) · Asian Journal of Andrology · doi:10.4103/1008-682x.156119 · Cited by 15 · see citing works
Tanihara, F., Nakai, M., Men, N. T., Kato, N., Kaneko, H., Noguchi, J., Otoi, T., & Kikuchi, K. (2014) · Animal Science Journal · doi:10.1111/asj.12164 · Cited by 14 · see citing works
Dynamics of the mammalian sperm membrane modification leading to fertilization: a cytological study
Toshimori, K. (2011) · Microscopy · doi:10.1093/jmicro/dfr036 · Cited by 14 · see citing works
Association of TUSC1 and DPF3 gene polymorphisms with male infertility
Sato, Y., Hasegawa, C., Tajima, A., Nozawa, S., Yoshiike, M., Koh, E., Kanaya, J., Namiki, M., Matsumiya, K., Tsujimura, A., et al. (2017) · Journal of Assisted Reproduction and Genetics · doi:10.1007/s10815-017-1052-x · Cited by 14 · see citing works
Cleavage of SPACA1 regulates assembly of sperm–egg membrane fusion machinery in mature spermatozoa†
Yamatoya, K., Kousaka, M., Ito, C., Nakata, K., Hatano, M., Araki, Y., & Toshimori, K. (2019) · Biology of Reproduction · doi:10.1093/biolre/ioz223 · Cited by 13 · see citing works
Derežanin, L., Blažytė, A., Dobrynin, P. V., Duchêne, D. A., Grau, J. H., Jeon, S., Kliver, S. F., Koepfli, K., Meneghini, D., Preick, M., et al. (2022) · Molecular Ecology · doi:10.1111/mec.16443 · Cited by 14 · see citing works
Role of complement regulatory proteins CD46, CD55 and CD59 in reproduction
Frolíková, M., Stopková, R., Antalíková, J., Johnson, P. M., Stopka, P., & Komrsková, K. (2012) · Folia Zoologica · doi:10.25225/fozo.v61.i1.a12.2012 · Cited by 12 · see citing works
Male infertility-related molecules involved in sperm-oocyte fusion
Mou, L., & Xie, N. (2016) · Journal of Reproduction and Development · doi:10.1262/jrd.2016-108 · Cited by 11 · see citing works
Caenorhabditis elegans sperm membrane protein interactome
Marcello, M. R., Druzhinina, M. K., & Singson, A. W. (2018) · Biology of Reproduction · doi:10.1093/biolre/ioy055 · Cited by 11 · see citing works
Molecular cloning and characterization of Izumo1 gene from bovine testis
Kim, E. (2015) · Journal of Animal Science and Technology · doi:10.1186/s40781-015-0049-1 · Cited by 9 · see citing works
Sperm IZUMO1-Dependent Gamete Fusion Influences Male Fertility in Mice
Saitô, T., Wada, I., & Inoue, N. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194809 · Cited by 8 · see citing works
Deep learning insights into the architecture of the mammalian egg-sperm fusion synapse
Elofsson, A., Han, L., Bianchi, E., Wright, G. J., & Jovine, L. (2024) · eLife · doi:10.7554/elife.93131.3 · Cited by 8 · see citing works
The Role of Tetraspanin Complexes in Egg-Sperm Fusion
Barraud‐Lange, V., & Boucheix, C. (2013) · Springer eBooks · doi:10.1007/978-94-007-6070-7_9 · Cited by 7 · see citing works
Expression Analysis of IZUMO1 Gene during Testicular Development of Datong Yak (Bos Grunniens)
Kalwar, Q., Ding, X., Ahmad, A. A., Chu, M., Wu, X., Bao, P., & Yan, P. (2019) · Animals · doi:10.3390/ani9060292 · Cited by 7 · see citing works
Subcellular localization of MS4A13 isoform 2 in mouse spermatozoa
Kaneko, T., Toshimori, K., & Iida, H. (2017) · Reproduction · doi:10.1530/rep-17-0477 · Cited by 6 · see citing works
Alternative splicing of the Izumo1 gene ensures triggering gamete fusion in mice
Saitô, T., Wada, I., & Inoue, N. (2019) · Scientific Reports · doi:10.1038/s41598-019-40130-7 · Cited by 6 · see citing works
Involvement of cellular protrusions in gamete interactions
Satouh, Y., & Inoue, N. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.031 · Cited by 6 · see citing works
Lu, Y., Ikawa, M., & Tang, S. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2425952122 · Cited by 5 · see citing works
Antisperm Contraceptive Vaccine
Naz, R. K. (2016) · Springer eBooks · doi:10.1007/978-3-319-40788-3_17 · Cited by 5 · see citing works
Recurrent Duplication and Diversification of Acrosomal Fertilization Proteins in Abalone
Carlisle, J. A., Glenski, M. A., & Swanson, W. J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.795273 · Cited by 5 · see citing works
Garcia‐Oliveros, L. N., Bozzi, A. D. R., Silva, T. D. O. C., Nascimento, F. B., de Oliveira, T. R., Miguel, E. L., Alves, M. B. R., Rangel, R. B., de Andrade, A. F. C., de Arruda, R. P., et al. (2025) · Cryobiology · doi:10.1016/j.cryobiol.2025.105302 · Cited by 4 · see citing works
Uncovering the Role of IZUMO Family Members in Human Fertilization
Manjon, A. A., Verón, G. L., Garay, S. A., Juarez, A., de Raffo, F. G. E., & Vazquez-Levin, M. H. (2025) · Molecular Reproduction and Development · doi:10.1002/mrd.70040 · Cited by 4 · see citing works
Marriage shrines and worms impacting our understanding of mammalian fertilization
Krauchunas, A. R., & Singson, A. W. (2016) · Worm · doi:10.1080/21624054.2016.1184389 · Cited by 4 · see citing works
Deep learning insights into the architecture of the mammalian egg-sperm fusion synapse
Elofsson, A., Han, L., Bianchi, E., Wright, G. J., & Jovine, L. (2023) · doi:10.1101/2023.07.27.550195 · Cited by 3 · see citing works
- Authors
- Ellerman, D. A., Pei, J., Gupta, S., Snell, W. J., Myles, D., & Primakoff, P.
- Affiliations
- University of California, Davis (US)
- Howard Hughes Medical Institute (US)
- The University of Texas Southwestern Medical Center (US)
- Corresponding author
- Ellerman, Diego A.
- Venue
- Molecular Reproduction and Development
- Publisher
- Wiley
- Published
- 2009-08-05
- Volume
- 76
- Issue
- 12
- Pages
- 1188-1199
- ISSN
- 1040-452X (ISSN-L)
- 1098-2795
- PMC
- PMC3779078
- OpenAlex
- W2063034367
- Cited by
- 143
- References
- 27
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 9 · 2023: 15 · 2022: 13 · 2021: 5 · 2020: 9 · 2019: 9 · 2018: 3 · 2017: 4 · 2016: 12 · 2015: 10 · 2014: 11 · 2013: 5 · 2012: 8
- FWCI
- 10.60
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular Reproduction and Development (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- U.S. Public Health Service (U54 29125, 16580)
- National Institute of General Medical Sciences (GM-56778, R01GM056778)
- Topics
- Health Sciences › Medicine › Reproductive Medicine › Sperm and Testicular Function
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Reproductive Biology and Fertility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Reproductive biology and impacts on aquatic species
- Keywords
- Izumo, sperm membrane proteins, gamete fusion, immunoglobulin domains, N-terminal domain, protein complexes, protein dimerization, protein oligomerization, testis-specific proteins
- MeSH terms
- Amino Acid Sequence, Animals, Cricetulus, Cricetinae, Humans, Immunoglobulins, Male, Membrane Proteins, Molecular Sequence Data, Recombinant Fusion Proteins, Spermatozoa, Sequence Alignment, CHO Cells, Protein Isoforms, Multiprotein Complexes, Mice, Protein Multimerization
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