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

ADP-Ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes.

The Journal of cell biology - 27 Jul 1998

Ooi C E, Dell'Angelica E C, Bonifacino J S

Abstract excerpt

Small GTP-binding proteins such as ADP- ribosylation factor 1 (ARF1) and Sar1p regulate the membrane association of coat proteins involved in intracellular membrane trafficking. ARF1 controls the clathrin coat adaptor AP-1 and the nonclathrin coat COPI, whereas Sar1p controls the nonclathrin coat COPII. In this study, we demonstrate that membrane association of the recently described AP-3 adaptor is regulated by...

Read the complete abstract on PubMed

Topics

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

Share to Anti-Bacterial Agents
Share to Brain
Share to Cattle

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

Share to Cells, Cultured

Share to GTP-Binding Proteins

Share to HeLa Cells

Share to In Vitro Techniques

Source

Open in PubMed Open full text

Identifiers

PMID: 9679139
DOI: 10.1083/jcb.142.2.391
PMCID: PMC2133064

Genes

ARF1
ARF5
ARF6

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

ADP-Ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes.PMID 9679139Read ↗

Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1.Semantic proximity Read ↗

Discrete determinants in ArfGAP2/3 conferring Golgi localization and regulation by the COPI coat.Semantic proximity Read ↗

Binding and functions of ADP-ribosylation factor on mammalian and yeast peroxisomes.Semantic proximity Read ↗

GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex.Semantic proximity Read ↗

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

Shared and specific functions of Arfs 1–5 at the Golgi revealed by systematic knockoutsSemantic proximity Read ↗

Effects of activated ADP-ribosylation factors on Golgi morphology require neither activation of phospholipase D1 nor recruitment of coatomer.Semantic proximity Read ↗

The ArfGAP Glo3 is required for the generation of COPI vesicles.Semantic proximity Read ↗

Epidermal growth factor-dependent phosphorylation of the GGA3 adaptor protein regulates its recruitment to membranes.Semantic proximity Read ↗

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

ADP-ribosylation factor 1 of Arabidopsis plays a critical role in intracellular trafficking and maintenance of endoplasmic reticulum morphology in Arabidopsis.Semantic proximity Read ↗

Phosphorylation-induced conformational changes regulate GGAs 1 and 3 function at the trans-Golgi network.Semantic proximity Read ↗

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