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

Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1.

Traffic (Copenhagen, Denmark) - 1 May 2005

Szul Tomasz, Garcia-Mata Rafael, Brandon Elizabeth, Shestopal Svetlana, Alvarez Cecilia, Sztul Elizabeth

Abstract excerpt

ADP-ribosylation factor (ARF)-facilitated recruitment of COP I to membranes is required for secretory traffic. The guanine nucleotide exchange factor GBF1 activates ARF and regulates ARF/COP I dynamics at the endoplasmic reticulum (ER)-Golgi interface. Like ARF and coatomer, GBF1 peripherally associates with membranes. ADP-ribosylation factor and coatomer have been shown to rapidly cycle between membranes and...

Read the complete abstract on PubMed

Topics

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

Share to ADP-Ribosylation Factors
Share to Brefeldin A

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Endoplasmic Reticulum

Share to Fluorescence Recovery After Photobleaching

Share to Golgi Apparatus

Share to Green Fluorescent Proteins

Share to Guanine Nucleotide Exchange Factors

Share to Protein Synthesis Inhibitors

Source

Identifiers

PMID: 15813748
DOI: 10.1111/j.1600-0854.2005.00282.x

Genes

GBF1
ARF1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1.PMID 15813748Read ↗

Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor at the Golgi.Semantic proximity Read ↗

Characterization of class I and II ADP-ribosylation factors (Arfs) in live cells: GDP-bound class II Arfs associate with the ER-Golgi intermediate compartment independently of GBF1.Semantic proximity Read ↗

BIG2, a guanine nucleotide exchange factor for ADP-ribosylation factors: its localization to recycling endosomes and implication in the endosome integrity.Semantic proximity Read ↗

In vivo monitoring of the recruitment and activation of AP-1 by Arf1.Semantic proximity Read ↗

Arf1 dissociates from the clathrin adaptor GGA prior to being inactivated by Arf GTPase-activating proteins.Semantic proximity Read ↗

Kinetic analysis of Arf GAP1 indicates a regulatory role for coatomer.Semantic proximity Read ↗

The ARF GTPases: defining roles in membrane traffic and organelle structure.Semantic proximity Read ↗

The KDEL receptor regulates a GTPase-activating protein for ADP-ribosylation factor 1 by interacting with its non-catalytic domain.Semantic proximity Read ↗

Role of coatomer and phospholipids in GTPase-activating protein-dependent hydrolysis of GTP by ADP-ribosylation factor-1.Semantic proximity Read ↗

ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation.Semantic proximity Read ↗

Overexpression of wild-type and mutant ARF1 and ARF6: distinct perturbations of nonoverlapping membrane compartments.Semantic proximity Read ↗

Gene editing and super-resolution microscopy reveal multiple distinct roles for ARF GTPases in cellular membrane organizationSemantic proximity Read ↗

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