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

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

Molecular and cellular neurosciences - 1 Jan 2020

Ruiter Marvin, Houy Sébastien, Engholm-Keller Kasper, Graham Mark E, Sørensen Jakob B

Abstract excerpt

SNAP-25, one of the three SNARE-proteins responsible for synaptic release, can be phosphorylated by Protein Kinase C on Ser-187, close to the fusion pore. In neuroendocrine cells, this phosphorylation event potentiates vesicle recruitment into releasable pools, whereas the consequences of phosphorylation for synaptic release remain unclear. We mutated Ser-187 and expressed two mutants (S187C and S187E) in the...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Excitatory Postsynaptic Potentials

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Neuronal Plasticity

Share to Phorbol Esters

Share to Protein Kinase C

Share to Rats, Wistar

Share to Serine

Share to Synaptosomal-Associated Protein 25

Source

Identifiers

PMID: 31794878
DOI: 10.1016/j.mcn.2019.103452

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

SNAP-25 phosphorylation at Ser187 is not involved in Ca2+ or phorbolester-dependent potentiation of synaptic release.PMID 31794878Read ↗

SNAP-25 phosphorylation at Ser187 regulates synaptic facilitation and short-term plasticity in an age-dependent manner.Semantic proximity Read ↗

Activity-dependent phosphorylation of Ser187 is required for SNAP-25-negative modulation of neuronal voltage-gated calcium channels.Semantic proximity Read ↗

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

Phosphorylation of SNAP-25 at Ser187 mediates enhancement of exocytosis by a phorbol ester in INS-1 cells.Semantic proximity Read ↗

Effects of PKA-mediated phosphorylation of Snapin on synaptic transmission in cultured hippocampal neurons.Semantic proximity Read ↗

SNAP-25 Ser187 does not mediate phorbol ester enhancement of hippocampal synaptic transmission.Semantic proximity Read ↗

Phosphorylation of SNAP-25 on serine-187 is induced by secretagogues in insulin-secreting cells, but is not correlated with insulin secretion.Semantic proximity Read ↗

SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions.Semantic proximity Read ↗

SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactionsSemantic proximity Read ↗

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

Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25.Semantic proximity Read ↗

Inhibition of SNAP-25 phosphorylation at Ser187 is involved in chronic morphine-induced down-regulation of SNARE complex formation.Semantic proximity Read ↗

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