ArticleThe Journal of cell biology1993
Two distinct populations of ARF bound to Golgi membranes.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 117 citations in OpenAlex.
- Lipid-anchored proteasomes control membrane protein homeostasis.Science advances · 2023Article
- VGLUT2 Trafficking Is Differentially Regulated by Adaptor Proteins AP-1 and AP-3.Frontiers in cellular neuroscience · 2017Article
- Retrograde vesicle transport in the Golgi.Protoplasma · 2012Review
- Several ADP-ribosylation factor (Arf) isoforms support COPI vesicle formation.The Journal of biological chemistry · 2011Article
- β-Subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK).Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Mechanisms of COPI vesicle formation.FEBS letters · 2009Review
- Structure and membrane interaction of myristoylated ARF1.Structure (London, England : 1993) · 2009Article
- Membrane curvature induced by Arf1-GTP is essential for vesicle formation.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Membrane metabolism mediated by Sec14 family members influences Arf GTPase activating protein activity for transport from the trans-Golgi.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation.The Journal of cell biology · 2005Article
- The ArfGAP Glo3 is required for the generation of COPI vesicles.Molecular biology of the cell · 2004Article
- ARF1.GTP, tyrosine-based signals, and phosphatidylinositol 4,5-bisphosphate constitute a minimal machinery to recruit the AP-1 clathrin adaptor to membranes.Molecular biology of the cell · 2002Article
- Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1.Molecular biology of the cell · 2002Article
- Recruitment to Golgi membranes of ADP-ribosylation factor 1 is mediated by the cytoplasmic domain of p23.The EMBO journal · 2001Article
- ADP-ribosylation factor and phosphatidic acid levels in Golgi membranes during budding of coatomer-coated vesicles.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- The molecular characterization of transport vesicles.Plant molecular biology · 1998Review
- Brefeldin A inhibits cell-free, de novo synthesis of poliovirus.Journal of virology · 1998Article
- ADP-Ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes.The Journal of cell biology · 1998Article
- ADP-ribosylation factor 1 transiently activates high-affinity adaptor protein complex AP-1 binding sites on Golgi membranes.Molecular biology of the cell · 1998Article
- Reversible dissociation of coatomer: functional characterization of a beta/delta-coat protein subcomplex.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ADP-ribosylation factor (ARF) is a small molecular weight GTP-binding protein (20 kD) and has been implicated in vesicular protein transport. The guanine nucleotide, bound to ARF protein is believed to modulate the activity of ARF but the mechanism of action remains elusive. We have previously reported that ARF binds to Golgi membranes after Brefeldin A-sensitive nucleotide exchange of ARF-bound GDP for GTP gamma S. Here we report that treatment with phosphatidylcholine liposomes effectively removed 40-60% of ARF bound to Golgi membranes with nonhydrolyzable GTP, presumably by competing for binding of activated ARF to lipid bilayers. This revealed the presence of two different pools of ARF on Golgi membranes. Whereas total ARF binding did not appear to be saturable, the liposome-resistant pool is saturable suggesting that this pool of ARF is stabilized by interaction with a Golgi membrane-component. We propose that activation of ARF by a guanine nucleotide-exchange protein results in association of myristoylated ARF GTP with the lipid bilayer of the Golgi apparatus. Once associated with the membrane, activated ARF can diffuse freely to associate stably with a target protein or possibly can be inactivated by a GTPase activating protein (GAP) activity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.