ArticleThe Journal of biological chemistry2011
Arfaptins are localized to the trans-Golgi by interaction with Arl1, but not Arfs.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed, 52 citations in OpenAlex.
- Lipid flippases ATP9A and ATP9B form a complex and contribute to the exocytic pathway from the Golgi.Life science alliance · 2025Article
- Substrates, regulation, cellular functions, and disease associations of P4-ATPases.Communications biology · 2025Review
- ATG9A shapes the forming autophagosome through Arfaptin 2 and phosphatidylinositol 4-kinase IIIβ.The Journal of cell biology · 2019Article
- Deciphering the BAR code of membrane modulators.Cellular and molecular life sciences : CMLS · 2017Review
- Depletion of the human N-terminal acetyltransferase hNaa30 disrupts Golgi integrity and ARFRP1 localization.Bioscience reports · 2017Article
- The phospholipid flippase ATP9A is required for the recycling pathway from the endosomes to the plasma membrane.Molecular biology of the cell · 2016Article
- BAR Domain-Containing FAM92 Proteins Interact with Chibby1 To Facilitate Ciliogenesis.Molecular and cellular biology · 2016Article
- Structural Insights into Arl1-Mediated Targeting of the Arf-GEF BIG1 to the trans-Golgi.Cell reports · 2016Article
- Protein Kinase D2 Assembles a Multiprotein Complex at the Trans-Golgi Network to Regulate Matrix Metalloproteinase Secretion.The Journal of biological chemistry · 2016Article
- The guanine exchange factor Gartenzwerg and the small GTPase Arl1 function in the same pathway with Arfaptin during synapse growth.Biology open · 2015Article
- Article
- Regulators and Effectors of Arf GTPases in Neutrophils.Journal of immunology research · 2015Review
- The Arf family G protein Arl1 is required for secretory granule biogenesis in Drosophila.Journal of cell science · 2014Article
- Serum proteomic analysis identifies sex-specific differences in lipid metabolism and inflammation profiles in adults diagnosed with Asperger syndrome.Molecular autism · 2014Article
- Recruitment of arfaptins to the trans-Golgi network by PI(4)P and their involvement in cargo export.The EMBO journal · 2013Article
- Normal dynactin complex function during synapse growth in Drosophila requires membrane binding by Arfaptin.Molecular biology of the cell · 2013Article
- Saving the neck from scission.Communicative & integrative biology · 2013Article
- Article
- Rab6a/a' are important Golgi regulators of pro-inflammatory TNF secretion in macrophages.PloS one · 2013Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arfaptins (arfaptin-1 and arfaptin-2/POR1) were originally identified as binding partners of the Arf small GTPases. Both proteins contain a BAR (Bin/Amphiphysin/Rvs) domain, which participates in membrane deformation. Here we show that arfaptins associate with trans-Golgi membranes. Unexpectedly, Arl1 (Arf-like 1), but not Arfs, determines the trans-Golgi association of arfaptins. We also demonstrate that arfaptins interact with Arl1 through their BAR domain-containing region and compete for Arl1 binding with golgin-97 and golgin-245/p230, both of which also bind to Arl1 through their GRIP (golgin-97/RanBP2/Imh1p/p230) domains. However, arfaptins and these golgins show only limited colocalization at the trans-Golgi. Time-lapse imaging of cells overexpressing fluorescent protein-tagged arfaptins and golgin-97 reveals that arfaptins, but not golgin-97, are included in vesicular and tubular structures emanating from the Golgi region. These observations indicate that arfaptins are recruited onto trans-Golgi membranes by interacting with Arl1, and capable of inducing membrane deformation via their BAR domains.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.