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

SCAMP2 interacts with Arf6 and phospholipase D1 and links their function to exocytotic fusion pore formation in PC12 cells.

Molecular biology of the cell - 1 Oct 2005

Liu Lixia, Liao Haini, Castle Anna, Zhang Jie, Casanova James, Szabo Gabor, Castle David

Abstract excerpt

SNAP receptor (SNARE)-mediated fusion is regarded as a core event in exocytosis. Exocytosis is supported by other proteins that set up SNARE interactions between secretory vesicle and plasma membranes or facilitate fusion pore formation. Secretory carrier membrane proteins (SCAMPs) are candidate proteins for functioning in these events. In neuroendocrine PC12 cells, SCAMP2 colocalizes on the cell surface with...

Read the complete abstract on PubMed

Topics

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

Share to ADP-Ribosylation Factor 6
Share to ADP-Ribosylation Factors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Membrane Permeability

Share to Exocytosis

Share to Guanosine 5'-O-(3-Thiotriphosphate)

Share to Norepinephrine

Share to PC12 Cells

Share to Phospholipase D

Source

Open in PubMed Open full text

Identifiers

PMID: 16030257
DOI: 10.1091/mbc.e05-03-0231
PMCID: PMC1237056

Genes

SCAMP2
PLD1

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

SCAMP2 interacts with Arf6 and phospholipase D1 and links their function to exocytotic fusion pore formation in PC12 cells.PMID 16030257Read ↗

Synaptotagmin-Ca2+ triggers two sequential steps in regulated exocytosis in rat PC12 cells: fusion pore opening and fusion pore dilation.Semantic proximity Read ↗

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

Membrane association domains in Ca2+-dependent activator protein for secretion mediate plasma membrane and dense-core vesicle binding required for Ca2+-dependent exocytosis.Semantic proximity Read ↗

Regulation of exocytosis and fusion pores by synaptotagmin-effector interactions.Semantic proximity Read ↗

Synaptotagmin-1 utilizes membrane bending and SNARE binding to drive fusion pore expansion.Semantic proximity Read ↗

Local protein dynamics during microvesicle exocytosis in neuroendocrine cells.Semantic proximity Read ↗

The Dual Function of the Polybasic Juxtamembrane Region of Syntaxin 1A in Clamping Spontaneous Release and Stimulating Ca2+-Triggered Release in Neuroendocrine Cells.Semantic proximity Read ↗

Control of fusion pore dynamics during exocytosis by Munc18.Semantic proximity Read ↗

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

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.Semantic proximity Read ↗

A gain-of-function mutant of Munc18-1 stimulates secretory granule recruitment and exocytosis and reveals a direct interaction of Munc18-1 with Rab3.Semantic proximity Read ↗

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

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