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Article

Blocking dephosphorylation at Serine 120 residue in t-SNARE SNAP-23 leads to massive inhibition in exocytosis from mast cells.

Journal of biosciences - 1 Mar 2018

Naskar Pieu, Naqvi Nilofer, Puri Niti

Abstract excerpt

Mast cells (MCs) respond to allergen challenge by release of pre-stored inflammatory mediators from their secretory granules, on cross-linking of Fc(epsilon) receptor I (Fc(epsilon)RI) receptors. The target-SNARE (t-SNARE) SNAP-23 has been shown to play an important role in MC exocytosis and undergoes transient phosphorylation at Serine 95 (S95) and Serine 120 (S120), concomitant with mediator release. During...

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PMID: 29485121

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

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Click a neighbor to travelStep 1 · 12 closest

Blocking dephosphorylation at Serine 120 residue in t-SNARE SNAP-23 leads to massive inhibition in exocytosis from mast cells.PMID 29485121Read ↗

Phosphorylation of SNAP-23 regulates exocytosis from mast cells.Semantic proximity Read ↗

Phosphomimetic mutation of cysteine string protein-α increases the rate of regulated exocytosis by modulating fusion pore dynamics in PC12 cells.Semantic proximity Read ↗

PKCε controls the fusion of secretory vesicles in mast cells in a phosphatidic acid-dependent mode.Semantic proximity Read ↗

Phosphomimetic mutation of Ser-187 of SNAP-25 increases both syntaxin binding and highly Ca2+-sensitive exocytosis.Semantic proximity Read ↗

Identification of three new splice variants of the SNARE protein SNAP-23.Semantic proximity Read ↗

The SNARE proteins SNAP-25 and SNAP-23 display different affinities for lipid rafts in PC12 cells. Regulation by distinct cysteine-rich domains.Semantic proximity Read ↗

Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis.Semantic proximity Read ↗

Gβγ inhibits exocytosis via interaction with critical residues on soluble N-ethylmaleimide-sensitive factor attachment protein-25.Semantic proximity Read ↗

SNAP-25 phosphorylation at Ser187 is not involved in Ca2+ or phorbolester-dependent potentiation of synaptic release.Semantic proximity Read ↗

Positively charged amino acids at the SNAP-25 C terminus determine fusion rates, fusion pore properties, and energetics of tight SNARE complex zippering.Semantic proximity Read ↗

Molecular analysis of SNAP-25 function in exocytosis.Semantic proximity Read ↗

The hydrophobic cysteine-rich domain of SNAP25 couples with downstream residues to mediate membrane interactions and recognition by DHHC palmitoyl transferases.Semantic proximity Read ↗

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