Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Phosphorylation of SNAP-23 regulates exocytosis from mast cells.

The Journal of biological chemistry - 25 Feb 2005

Hepp Régine, Puri Niti, Hohenstein Anita C, Crawford Garland L, Whiteheart Sidney W, Roche Paul A

Abstract excerpt

Regulated exocytosis is a process in which a physiological trigger initiates the translocation, docking, and fusion of secretory granules with the plasma membrane. A class of proteins termed SNAREs (including SNAP-23, syntaxins, and VAMPs) are known regulators of secretory granule/plasma membrane fusion events. We have investigated the molecular mechanisms of regulated exocytosis in mast cells and find that...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Blood Platelets
Share to Exocytosis
Share to Mast Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Qa-SNARE Proteins

Share to R-SNARE Proteins

Share to Serine

Share to SNARE Proteins

Share to Vesicular Transport Proteins

Source

Identifiers

PMID: 15611044
DOI: 10.1074/jbc.M412126200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phosphorylation of SNAP-23 regulates exocytosis from mast cells.PMID 15611044Read ↗

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

EBAG9 Adds a New Layer of Control on Large Dense-Core Vesicle Exocytosis via Interaction with SnapinSemantic proximity Read ↗

The functions of Munc18-1 in regulated exocytosis.Semantic proximity Read ↗

Differential control of the releasable vesicle pools by SNAP-25 splice variants and SNAP-23.Semantic proximity Read ↗

Molecular analysis of SNAP-25 function in exocytosis.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 ↗

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

Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosisSemantic proximity Read ↗

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

⌁Select a neighboring publication to make it the new centre.