ArticlePloS one2011
α-SNAP prevents docking of the acrosome during sperm exocytosis because it sequesters monomeric syntaxin.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 41 citations in OpenAlex.
- α-Synuclein is required for sperm exocytosis at a post-fusion stage.Frontiers in cell and developmental biology · 2023Article
- Munc18-1 is crucial to overcome the inhibition of synaptic vesicle fusion by αSNAP.Nature communications · 2019Article
- Mechanism of Acrosome Biogenesis in Mammals.Frontiers in cell and developmental biology · 2019Review
- NaeLife · 2017Article
- Components of the SNARE-containing regulon are co-regulated in root cells undergoing defense.Plant signaling & behavior · 2017Article
- The Rab3A-22A Chimera Prevents Sperm Exocytosis by Stabilizing Open Fusion Pores.The Journal of biological chemistry · 2016Article
- Expression of Syntaxin 2 in Bovine Sperm.Journal of cellular biology & molecular sciences · 2016Article
- PKA-dependent phosphorylation of LIMK1 and Cofilin is essential for mouse sperm acrosomal exocytosis.Developmental biology · 2015Article
- Article
- The syntaxin 31-induced gene, LESION SIMULATING DISEASE1 (LSD1), functions in Glycine max defense to the root parasite Heterodera glycines.Plant signaling & behavior · 2015Article
- α-SNAP interferes with the zippering of the SNARE protein membrane fusion machinery.The Journal of biological chemistry · 2014Article
- Syntaxin 31 functions in Glycine max resistance to the plant parasitic nematode Heterodera glycines.Plant molecular biology · 2014Article
- Syncytin-1 and its receptor is present in human gametes.Journal of assisted reproduction and genetics · 2014Article
- Unresolved questions concerning mammalian sperm acrosomal exocytosis.Biology of reproduction · 2014Review
- Sustained high protein-tyrosine phosphatase 1B activity in the sperm of obese males impairs the sperm acrosome reaction.The Journal of biological chemistry · 2014Article
- Article
- Munc18-1 controls SNARE protein complex assembly during human sperm acrosomal exocytosis.The Journal of biological chemistry · 2012Article
- The expression of a naturally occurring, truncated allele of an α-SNAP gene suppresses plant parasitic nematode infection.Plant molecular biology · 2012Article
- Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-SNAP has an essential role in membrane fusion that consists of bridging cis SNARE complexes to NSF. α-SNAP stimulates NSF, which releases itself, α-SNAP, and individual SNAREs that subsequently re-engage in the trans arrays indispensable for fusion. α-SNAP also binds monomeric syntaxin and NSF disengages the α-SNAP/syntaxin dimer. Here, we examine why recombinant α-SNAP blocks secretion in permeabilized human sperm despite the fact that the endogenous protein is essential for membrane fusion. The only mammalian organism with a genetically modified α-SNAP is the hyh mouse strain, which bears a M105I point mutation; males are subfertile due to defective sperm exocytosis. We report here that recombinant α-SNAP-M105I has greater affinity for the cytosolic portion of immunoprecipitated syntaxin than the wild type protein and in consequence NSF is less efficient in releasing the mutant. α-SNAP-M105I is a more potent sperm exocytosis blocker than the wild type and requires higher concentrations of NSF to rescue its effect. Unlike other fusion scenarios where SNAREs are subjected to an assembly/disassembly cycle, the fusion machinery in sperm is tuned so that SNAREs progress uni-directionally from a cis configuration in resting cells to monomeric and subsequently trans arrays in cells challenged with exocytosis inducers. By means of functional and indirect immunofluorescense assays, we show that recombinant α-SNAPs--wild type and M105I--inhibit exocytosis because they bind monomeric syntaxin and prevent this SNARE from assembling with its cognates in trans. Sequestration of free syntaxin impedes docking of the acrosome to the plasma membrane assessed by transmission electron microscopy. The N-terminal deletion mutant α-SNAP-(160-295), unable to bind syntaxin, affects neither docking nor secretion. The implications of this study are twofold: our findings explain the fertility defect of hyh mice and indicate that assembly of SNAREs in trans complexes is essential for docking.
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