ArticleJournal of cell science2011
Phospholipase Cζ binding to PtdIns(4,5)P2 requires the XY-linker region.
Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed, 72 citations in OpenAlex.
- A catalytically competent sperm PLCzeta variant causes fertilization failure through protein insufficiency.Journal of assisted reproduction and genetics · 2026Article
- Pathogenic homozygous PLCZ1 mutation reduces sperm protein levels with a simulated reduction of PIP2 binding: a case report.Reproduction & fertility · 2026Article
- A Novel PLCζ Mutation Linked to Male Factor Infertility Induces a Gain-of-Function Effect on CaInternational journal of molecular sciences · 2025Article
- Mammalian PI-Phospholipase C Isozymes: Structural and Functional Insights and Roles in Health and Disease.Medicina (Kaunas, Lithuania) · 2025Review
- Phospholipase Cζ, the Molecular Spark of Fertilization and Male Infertility: Insights from Bench to Bedside.Medicina (Kaunas, Lithuania) · 2025Review
- Structural Implications of H233L and H398P Mutations in Phospholipase Cζ: A Full-Atom Molecular Dynamics Study on Infertility-Associated Dysfunctions.International journal of molecular sciences · 2025Article
- Phospholipase C zeta: a hidden face of sperm for oocyte activation and early embryonic development.Obstetrics & gynecology science · 2024Article
- Molecular Mechanism of Oocyte Activation in Mammals: Past, Present, and Future Directions.Biomolecules · 2024Review
- ZneLife · 2023Article
- Phospholipase C Zeta 1 (PLCZ1): The Function and Potential for Fertility Assessment and In Vitro Embryo Production in Cattle and Horses.Veterinary sciences · 2023Review
- ZnbioRxiv : the preprint server for biology · 2023Article
- Selection of fertilization strategies for different sperm parameters in vitro fertilization.Annals of translational medicine · 2022Article
- Emerging role of phospholipase C mediated lipid signaling in abiotic stress tolerance and development in plants.Plant cell reports · 2021Review
- Impact of Cryopreservation on Spermatozoa Freeze-Thawed Traits and Relevance OMICS to Assess Sperm Cryo-Tolerance in Farm Animals.Frontiers in veterinary science · 2021Review
- Modulators of calcium signalling at fertilization.Open biology · 2020Review
- Essential Role of Sperm-Specific PLC-Zeta in Egg Activation and Male Factor Infertility: An Update.Frontiers in cell and developmental biology · 2020Review
- CaCold Spring Harbor perspectives in biology · 2019Review
- The eggstraordinary story of how life begins.Molecular reproduction and development · 2019Review
- Calcium influx and sperm-evoked calcium responses during oocyte maturation and egg activation.Oncotarget · 2017Review
- Occurrence and functional significance of the transcriptome in bovine (Bos taurus) spermatozoa.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Phospholipase C-zeta (PLCζ) is a strong candidate for the mammalian sperm-derived factor that triggers the Ca(2+) oscillations required for egg activation at fertilization. PLCζ lacks a PH domain, which targets PLCδ1 to the phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)) substrate in the plasma membrane. Previous studies failed to detect PLCζ in the plasma membrane, hence the means of PLCζ binding to PtdIns(4,5)P(2) is unclear. We find that the PLCζ XY linker, but not the C2 domain, exhibits robust binding to PtdIns(4,5)P(2) or to liposomes containing near-physiological levels of PtdIns(4,5)P(2). The role of positively charged residues within the XY linker was addressed by sequentially substituting alanines for three lysine residues, K374, K375 and K377. Microinjection of these mutants into mouse eggs enabled their Ca(2+) oscillation-inducing activities to be compared with wild-type PLCζ. The XY-linker mutant proteins were purified and the in vitro PtdIns(4,5)P(2) hydrolysis and binding properties were monitored. Successive reduction of net positive charge within the PLCζ XY linker significantly affects both in vivo Ca(2+)-oscillation-inducing activity and in vitro PtdIns(4,5)P(2) interaction of mouse PLCζ. Our data suggest that positively charged residues within the XY linker play an important role in the PLCζ interaction with PtdIns(4,5)P(2), a crucial step in generating the Ca(2+) activation signal that is essential for fertilization in mammals.
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Registered trials
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.