ArticleThe Journal of cell biology2000
Synaptotagmin VII regulates Ca(2+)-dependent exocytosis of lysosomes in fibroblasts.
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 143 papers.
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143 citing papers in PubMed, 305 citations in OpenAlex.
- Subtype-specific secretion of extracellular vesicles by LRRK2 and Rab GTPases under lysosomal stress.iScience · 2026Article
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- Exosomes are specialized vehicles to induce fibronectin assembly.bioRxiv : the preprint server for biology · 2025Article
- Identification of the role of SNARE proteins in rAAV vector production through interaction with the viral MAAP.Molecular therapy. Methods & clinical development · 2025Article
- Canonical and noncanonical autophagy: involvement in Parkinson's disease.Frontiers in cell and developmental biology · 2025Review
- The endolysosomal system in conventional and unconventional protein secretion.The Journal of cell biology · 2024Review
- The 8-oxoguanine DNA glycosylase-synaptotagmin 7 pathway increases extracellular vesicle release and promotes tumour metastasis during oxidative stress.Journal of extracellular vesicles · 2024Article
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- Wound Repair of the Cell Membrane: Lessons fromCells · 2024Review
- Synaptotagmin 7 C2 domains induce membrane curvature stress via electrostatic interactions and the wedge mechanism.bioRxiv : the preprint server for biology · 2024Article
- The lysosomal trafficking regulator "LYST": an 80-year traffic jam.Frontiers in immunology · 2024Review
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- Synaptotagmin-7 outperforms synaptotagmin-1 to promote the formation of large, stable fusion pores via robust membrane penetration.Nature communications · 2023Article
- Protrudin-mediated ER-endosome contact sites promote phagocytosis.Cellular and molecular life sciences : CMLS · 2023Article
- Role of calcium-sensor proteins in cell membrane repair.Bioscience reports · 2023Review
- Repair of traumatic lesions to the plasmalemma of neurons and other cells: Commonalities, conflicts, and controversies.Frontiers in physiology · 2023Review
- Four distinct cytoplasmic structures generate and release specific vesicles, thus opening the way to intercellular communication.Extracellular vesicles and circulating nucleic acids · 2023Review
- Lysosomal exocytosis releases pathogenic α-synuclein species from neurons in synucleinopathy models.Nature communications · 2022Article
83 more citing papers are in PubMed but not listed here.
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6 authors at 1 institution in 1 country.
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Abstract
Synaptotagmins (Syts) are transmembrane proteins with two Ca(2+)-binding C(2) domains in their cytosolic region. Syt I, the most widely studied isoform, has been proposed to function as a Ca(2+) sensor in synaptic vesicle exocytosis. Several of the twelve known Syts are expressed primarily in brain, while a few are ubiquitous (Sudhof, T.C., and J. Rizo. 1996. Neuron. 17: 379-388; Butz, S., R. Fernandez-Chacon, F. Schmitz, R. Jahn, and T.C. Sudhof. 1999. J. Biol. Chem. 274:18290-18296). The ubiquitously expressed Syt VII binds syntaxin at free Ca(2+) concentrations ([Ca(2+)]) below 10 microM, whereas other isoforms require 200-500 microM [Ca(2+)] or show no Ca(2+)-dependent syntaxin binding (Li, C., B. Ullrich, Z. Zhang, R.G.W. Anderson, N. Brose, and T.C. Sudhof. 1995. Nature. 375:594-599). We investigated the involvement of Syt VII in the exocytosis of lysosomes, which is triggered in several cell types at 1-5 microM [Ca(2+)] (Rodríguez, A., P. Webster, J. Ortego, and N.W. Andrews. 1997. J. Cell Biol. 137:93-104). Here, we show that Syt VII is localized on dense lysosomes in normal rat kidney (NRK) fibroblasts, and that GFP-tagged Syt VII is targeted to lysosomes after transfection. Recombinant fragments containing the C(2)A domain of Syt VII inhibit Ca(2+)-triggered secretion of beta-hexosaminidase and surface translocation of Lgp120, whereas the C(2)A domain of the neuronal- specific isoform, Syt I, has no effect. Antibodies against the Syt VII C(2)A domain are also inhibitory in both assays, indicating that Syt VII plays a key role in the regulation of Ca(2+)-dependent lysosome exocytosis.
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