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

Structural characterization of the Rabphilin-3A-SNAP25 interaction.

Proceedings of the National Academy of Sciences of the United States of America - 3 Jul 2017

Ferrer-Orta Cristina, Pérez-Sánchez María Dolores, Coronado-Parra Teresa, Silva Cristina, López-Martínez David, Baltanás-Copado Jesús, Gómez-Fernández Juan Carmelo, Corbalán-García Senena, Verdaguer Núria

Abstract excerpt

Membrane fusion is essential in a myriad of eukaryotic cell biological processes, including the synaptic transmission. Rabphilin-3A is a membrane trafficking protein involved in the calcium-dependent regulation of secretory vesicle exocytosis in neurons and neuroendocrine cells, but the underlying mechanism remains poorly understood. Here, we report the crystal structures and biochemical analyses of Rabphilin-3A...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Exocytosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Protein Domains

Share to Secretory Vesicles

Share to Synaptosomal-Associated Protein 25

Share to Syntaxin 1

Share to Vesicular Transport Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 28634303
DOI: 10.1073/pnas.1702542114
PMCID: PMC5502619

Genes

SNAP25

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

Structural characterization of the Rabphilin-3A-SNAP25 interaction.PMID 28634303Read ↗

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

The C2 domains of synaptotagmin--partners in exocytosis.Semantic proximity Read ↗

Fusion pore dynamics are regulated by synaptotagmin*t-SNARE interactions.Semantic proximity Read ↗

SNARE complex formation is triggered by Ca2+ and drives membrane fusion.Semantic proximity Read ↗

Localization of Rab3A-binding site on C2A domain of synaptotagmin I to reveal its regulatory mechanism.Semantic proximity Read ↗

The polybasic sequence in the C2B domain of rabphilin is required for the vesicle docking step in PC12 cells.Semantic proximity Read ↗

Synaptotagmin C2A loop 2 mediates Ca2+-dependent SNARE interactions essential for Ca2+-triggered vesicle exocytosis.Semantic proximity Read ↗

Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis.Semantic proximity Read ↗

Vesicle docking and fusion pore modulation by the neuronal calcium sensor Synaptotagmin-1Semantic proximity Read ↗

Conserved prefusion protein assembly in regulated exocytosis.Semantic proximity Read ↗

A Post-Docking Role of Synaptotagmin 1-C2B Domain Bottom Residues R398/399 in Mouse Chromaffin Cells.Semantic proximity Read ↗

Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening.Semantic proximity Read ↗

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