ADP-ribosylation factor is functionally and physically associated with the Golgi complex.

doi:10.1073/pnas.87.3.1238

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Article

ADP-ribosylation factor is functionally and physically associated with the Golgi complex.

Proceedings of the National Academy of Sciences of the United States of America - 1 Feb 1990

Stearns T, Willingham M C, Botstein D, Kahn R A

Abstract excerpt

ADP-ribosylation factor (ARF) is a ubiquitous, highly conserved 21-kDa GTP-binding protein, first identified in animal cells as the cofactor required for the in vitro ADP-ribosylation of the stimulatory regulatory subunit of adenylate cyclase, Gs, by cholera toxin. As the relevance of this activity to in vivo function is unknown, we have taken advantage of the conserved nature of ARF to study its function in...

Topics

ADP-Ribosylation Factor 1
ADP-Ribosylation Factors
Adenylyl Cyclases
Animals
Cells, Cultured
Enzyme Induction
Fluorescent Antibody Technique
GTP-Binding Proteins
Genes
Genes, Fungal
Glycoside Hydrolases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Golgi Apparatus

Immunohistochemistry

Kinetics

Membrane Proteins

Mice

Microscopy, Electron

Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 2105501
DOI: 10.1073/pnas.87.3.1238
PMCID: PMC53446

Genes

ARF1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2105501-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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