ArticleThe Journal of biological chemistry2009
PTP1B dephosphorylates N-ethylmaleimide-sensitive factor and elicits SNARE complex disassembly during human sperm exocytosis.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 47 citations in OpenAlex.
- α-Synuclein is required for sperm exocytosis at a post-fusion stage.Frontiers in cell and developmental biology · 2023Article
- The Emerging Role of Rab5 in Membrane Receptor Trafficking and Signaling Pathways.Biochemistry research international · 2020Review
- Dopamine D1A directly interacts with otoferlin synaptic pathway proteins: Ca2+ and phosphorylation underlie an NSF-to-AP2mu1 molecular switch.The Biochemical journal · 2017Article
- Article
- Protein tyrosine phosphatase 1B impairs diabetic wound healing through vascular endothelial growth factor receptor 2 dephosphorylation.Arteriosclerosis, thrombosis, and vascular biology · 2015Article
- Epac, Rap and Rab3 act in concert to mobilize calcium from sperm's acrosome during exocytosis.Cell communication and signaling : CCS · 2014Article
- Sustained high protein-tyrosine phosphatase 1B activity in the sperm of obese males impairs the sperm acrosome reaction.The Journal of biological chemistry · 2014Article
- Isolation of a calcium-binding protein of the acrosomal membrane of bovine spermatozoa.The international journal of biochemistry & cell biology · 2013Article
- Munc18-1 controls SNARE protein complex assembly during human sperm acrosomal exocytosis.The Journal of biological chemistry · 2012Article
- Protein-tyrosine kinase signaling in the biological functions associated with sperm.Journal of signal transduction · 2012Article
- Protein-tyrosine phosphatase 1B modulates early endosome fusion and trafficking of Met and epidermal growth factor receptors.The Journal of biological chemistry · 2011Article
- α-SNAP prevents docking of the acrosome during sperm exocytosis because it sequesters monomeric syntaxin.PloS one · 2011Article
- Characteristics of highly polymorphic segmental copy-number variations observed in Japanese by BAC-array-CGH.Journal of biomedicine & biotechnology · 2011Article
- Calcineurin-mediated dephosphorylation of synaptotagmin VI is necessary for acrosomal exocytosis.The Journal of biological chemistry · 2010Article
- Epac activates the small G proteins Rap1 and Rab3A to achieve exocytosis.The Journal of biological chemistry · 2009Article
- Ca2+-stores in sperm: their identities and functions.Reproduction (Cambridge, England) · 2009Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The reversible phosphorylation of tyrosyl residues in proteins is a cornerstone of the signaling pathways that regulate numerous cellular responses. Protein tyrosine phosphorylation is controlled through the concerted actions of protein-tyrosine kinases and phosphatases. The goal of the present study was to unveil the mechanisms by which protein tyrosine dephosphorylation modulates secretion. The acrosome reaction, a specialized type of regulated exocytosis undergone by sperm, is initiated by calcium and carried out by a number of players, including tyrosine kinases and phosphatases, and fusion-related proteins such as Rab3A, alpha-SNAP, N-ethylmaleimide-sensitive factor (NSF), SNAREs, complexin, and synaptotagmin VI. We report here that inducers were unable to elicit the acrosome reaction when permeabilized human sperm were loaded with anti-PTP1B antibodies or with the dominant-negative mutant PTP1B D181A; subsequent introduction of wild type PTP1B or NSF rescued exocytosis. Wild type PTP1B, but not PTP1B D181A, caused cis SNARE complex dissociation during the acrosome reaction through a mechanism involving NSF. Unlike its non-phosphorylated counterpart, recombinant phospho-NSF failed to dissociate SNARE complexes from rat brain membranes. These results strengthen our previous observation that NSF activity is regulated rather than constitutive during sperm exocytosis and indicate that NSF must be dephosphorylated by PTP1B to disassemble SNARE complexes. Interestingly, phospho-NSF served as a substrate for PTP1B in an in vitro assay. Our findings demonstrate that phosphorylation of NSF on tyrosine residues prevents its SNARE complex dissociation activity and establish for the first time a role for PTP1B in the modulation of the membrane fusion machinery.
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