ArticleDevelopment (Cambridge, England)2015
The cytoplasmic domain of the gamete membrane fusion protein HAP2 targets the protein to the fusion site in Chlamydomonas and regulates the fusion reaction.
Article in Development (Cambridge, England), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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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.
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Who cites it
28 citing papers in PubMed, 41 citations in OpenAlex.
- Molecular determinants of species-specific gamete adhesion triggering HAP2-mediated membrane fusion.Nature communications · 2026Article
- Vaccination of cattle with the Babesia bovis sexual-stage protein HAP2 abrogates parasite transmission by Rhipicephalus microplus ticks.NPJ vaccines · 2023Article
- Characteristics of NGenomics, proteomics & bioinformatics · 2023Article
- Behavior of Male Gamete Fusogen GCS1/HAP2 and the Regulation inBiomolecules · 2023Article
- Eukaryotic fertilization and gamete fusion at a glance.Journal of cell science · 2022Article
- DMP8 and 9 regulate HAP2/GCS1 trafficking for the timely acquisition of sperm fusion competence.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Malaria parasites utilize two essential plasma membrane fusogens for gamete fertilization.Cellular and molecular life sciences : CMLS · 2022Article
- Discovery of archaeal fusexins homologous to eukaryotic HAP2/GCS1 gamete fusion proteins.Nature communications · 2022Article
- Virus-Induced Membrane Fusion in Neurodegenerative Disorders.Frontiers in cellular and infection microbiology · 2022Review
- MAR1 links membrane adhesion to membrane merger during cell-cell fusion in Chlamydomonas.Developmental cell · 2021Article
- Species-specific gamete recognition initiates fusion-driving trimer formation by conserved fusogen HAP2.Nature communications · 2021Article
- Sequential production of gametes during meiosis in trypanosomes.Communications biology · 2021Article
- HAP2-Mediated Gamete Fusion: Lessons From the World of Unicellular Eukaryotes.Frontiers in cell and developmental biology · 2021Review
- The molecular foundations of zygosis.Cellular and molecular life sciences : CMLS · 2020Review
- Life cycle progression and sexual development of the apicomplexan parasite Cryptosporidium parvum.Nature microbiology · 2019Article
- How cells fuse.The Journal of cell biology · 2019Review
- Comparative Genomics Supports Sex and Meiosis in Diverse Amoebozoa.Genome biology and evolution · 2018Article
- Article
- Evolutionary diversification of the HAP2 membrane insertion motifs to drive gamete fusion across eukaryotes.PLoS biology · 2018Article
- Hap2, a novel gene in Babesia bigemina is expressed in tick stages, and specific antibodies block zygote formation.Parasites & vectors · 2017Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Cell-cell fusion between gametes is a defining step during development of eukaryotes, yet we know little about the cellular and molecular mechanisms of the gamete membrane fusion reaction. HAP2 is the sole gamete-specific protein in any system that is broadly conserved and shown by gene disruption to be essential for gamete fusion. The wide evolutionary distribution of HAP2 (also known as GCS1) indicates it was present in the last eukaryotic common ancestor and, therefore, dissecting its molecular properties should provide new insights into fundamental features of fertilization. HAP2 acts at a step after membrane adhesion, presumably directly in the merger of the lipid bilayers. Here, we use the unicellular alga Chlamydomonas to characterize contributions of key regions of HAP2 to protein location and function. We report that mutation of three strongly conserved residues in the ectodomain has no effect on targeting or fusion, although short deletions that include those residues block surface expression and fusion. Furthermore, HAP2 lacking a 237-residue segment of the cytoplasmic region is expressed at the cell surface, but fails to localize at the apical membrane patch specialized for fusion and fails to rescue fusion. Finally, we provide evidence that the ancient HAP2 contained a juxta-membrane, multi-cysteine motif in its cytoplasmic region, and that mutation of a cysteine dyad in this motif preserves protein localization, but substantially impairs HAP2 fusion activity. Thus, the ectodomain of HAP2 is essential for its surface expression, and the cytoplasmic region targets HAP2 to the site of fusion and regulates the fusion reaction.
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