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

αII-spectrin controls calcium-regulated exocytosis in neuroendocrine chromaffin cells through neuronal Wiskott-Aldrich Syndrome protein interaction.

IUBMB life - 1 Apr 2020

Houy Sébastien, Nicolas Gaël, Momboisse Fanny, Malacombe Magali, Bader Marie-France, Vitale Nicolas, Lecomte Marie-Christine, Ory Stéphane, Gasman Stéphane

Abstract excerpt

Besides a fundamental structural role at the plasma membrane, spectrin- and actin-based skeletons have been proposed to participate in various processes including vesicular trafficking. Neuroendocrine cells release hormones and neuropeptides through calcium-regulated exocytosis, a process that is coordinated by a fine remodeling of the actin cytoskeleton. We describe here that calcium-regulated exocytosis is...

Read the complete abstract on PubMed

Topics

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

Share to Catecholamines
Share to Chromaffin Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Exocytosis

Share to Growth Hormone

Share to Microfilament Proteins

Share to PC12 Cells

Share to src Homology Domains

Share to Two-Hybrid System Techniques

Source

Identifiers

PMID: 31859439
DOI: 10.1002/iub.2217

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

αII-spectrin controls calcium-regulated exocytosis in neuroendocrine chromaffin cells through neuronal Wiskott-Aldrich Syndrome protein interaction.PMID 31859439Read ↗

Structural and mechanistic insights into secretagogin-mediated exocytosis.Semantic proximity Read ↗

Syndapin 3 modulates fusion pore expansion in mouse neuroendocrine chromaffin cells.Semantic proximity Read ↗

Identification of secretory granule phosphatidylinositol 4,5-bisphosphate-interacting proteins using an affinity pulldown strategy.Semantic proximity Read ↗

Synaptotagmin oligomerization is essential for calcium control of regulated exocytosis.Semantic proximity Read ↗

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

Role of secretory carrier membrane protein SCAMP2 in granule exocytosis.Semantic proximity Read ↗

Targeted deletion of betaIII spectrin impairs synaptogenesis and generates ataxic and seizure phenotypes.Semantic proximity Read ↗

Synaptophysin: leading actor or walk-on role in synaptic vesicle exocytosis?Semantic proximity Read ↗

Binding of the complexin N terminus to the SNARE complex potentiates synaptic-vesicle fusogenicity.Semantic proximity Read ↗

Exophilin4/Slp2-a targets glucagon granules to the plasma membrane through unique Ca2+-inhibitory phospholipid-binding activity of the C2A domain.Semantic proximity Read ↗

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

Altered synaptobrevin-II trafficking in neurons expressing a synaptophysin mutation associated with a severe neurodevelopmental disorder.Semantic proximity Read ↗

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