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ADP-ribosylation factor 1

ARF1, ADP-ribosylation factor, ADP-Ribosylation Factor 1
ADP-ribosylation factor 1 (ARF1) is a member of the human ARF gene family. The family members encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking as activators of phospholipase D. The gene products, including 6 ARF proteins and 11 ARF-like proteins, constitute a family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1, ARF2 and ARF3), class II (ARF4 and ARF5) and class III (ARF6), and members of each class share a common gene organization. The ARF1 protein is localized to the Golgi apparatus and has a central role in intra-Golgi transport. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: p16, ARF6, CAN, Actin, V1a
Papers using ARF1 antibodies
Transcriptional regulatory networks in cellular responses and tolerance to dehydration and cold stress
Hoefgen Rainer et al., In Journal of Experimental Botany, 2003
... ARF1-BP coding regions (locus numbers At2g33310, At5g25890, At5g62010, respectively) employing the Advantage–HF2 PCR Kit (Clontech, Heidelberg, Germany) according to ...
Cell cycle-dependent localization of monoclonal antibodies raised against isolated Dictyostelium centrosomes.
Bassham Diane, In PLoS ONE, 1998
... The rabbit anti-Arf monoclonal antibody (clone ID EP442Y) directed against a peptide of Arf1 conserved in Dd-ArfA was purchased from Epitomics (Fermentas, France) ...
Papers on ARF1
MARTX effector cross kingdom activation by Golgi-associated ADP-ribosylation factors.
Satchell et al., Chicago, United States. In Cell Microbiol, Feb 2016
DmXVv was found to localize to Golgi and to directly interact with Golgi-associated ADP-ribosylation factors ARF1, ARF3, and ARF4, although ARF binding was not necessary for the subcellular localization.
Small GTPases in peroxisome dynamics.
Peränen et al., Heidelberg, Germany. In Biochim Biophys Acta, Feb 2016
The small GTPase ADP-ribosylation factor 1 (Arf1), for example, is known to stimulate synthesis of PI4P and PI(4,5)P2 on the Golgi to regulate protein and lipid sorting.
A novel splicing mutation in the IQSEC2 gene that modulates the phenotype severity in a family with intellectual disability.
Mila et al., Barcelona, Spain. In Eur J Hum Genet, Feb 2016
UNASSIGNED: The IQSEC2 gene is located on chromosome Xp11.22 and encodes a guanine nucleotide exchange factor for the ADP-ribosylation factor family of small GTPases.
Arf6 controls platelet spreading and clot retraction via integrin αIIbβ3 trafficking.
Whiteheart et al., Lexington, United States. In Blood, Feb 2016
ADP-ribosylation factor 6 (Arf6) is a small GTP-binding protein known to regulate endocytic trafficking, especially of integrins.
The Prediction of the Expected Current Selection Coefficient of Single Nucleotide Polymorphism Associated with Holstein Milk Yield, Fat and Protein Contents.
Kim et al., Seoul, South Korea. In Asian-australas J Anim Sci, Jan 2016
They are phosphodiesterase 4B (PDE4B), serine/threonine kinase 40 (STK40), collagen, type XI, alpha 1 (COL11A1), ephrin-A1 (EFNA1), netrin 4 (NTN4), neuron specific gene family member 1 (NSG1), estrogen receptor 1 (ESR1), neurexin 3 (NRXN3), spectrin, beta, non-erythrocytic 1 (SPTBN1), ADP-ribosylation factor interacting protein 1 (ARFIP1), mutL homolog 1 (MLH1), transmembrane channel-like 7 (TMC7), carboxypeptidase X, member 2 (CPXM2) and ADAM metallopeptidase domain 12 (ADAM12).
Amino acid sensing and activation of mechanistic target of rapamycin complex 1: implications for skeletal muscle.
Koopman et al., Melbourne, Australia. In Curr Opin Clin Nutr Metab Care, Jan 2016
The mechanisms of amino acid sensing and mTORC1 signaling are emerging with multiple potential sensors (e.g., solute carrier family 38, member 9, lysosomal protein transmembrane 4 beta/solute carrier family 7, member 5-solute carrier family 3, member 2) and signal transducers (e.g., Sestrins, ADP-ribosylation factor 1, and microspherule protein 1) identified.
Clinical and prognostic significance of Arl4c expression in colorectal cancer.
Xu et al., In Cancer Biomark, Jan 2016
BACKGROUND: ADP-ribosylation factor (ARF)-like 4c (Arl4c) has been reported to promote tumorigenesis in colorectal and lung cancers and may represent a novel therapeutic target.
Cargo adaptors: structures illuminate mechanisms regulating vesicle biogenesis.
Fromme et al., Ithaca, United States. In Trends Cell Biol, Jul 2015
Several different cargo adaptors functioning in distinct trafficking pathways at the Golgi are similarly regulated through bivalent binding to the ADP-ribosylation factor 1 (Arf1) GTPase, potentially enabling regulation by a threshold concentration of Arf1.
The PB1 domain in auxin response factor and Aux/IAA proteins: a versatile protein interaction module in the auxin response.
Guilfoyle, United States. In Plant Cell, 2015
In addition to the PB1 domain, a second protein interaction module that functions in ARF-ARF dimerization and facilitates DNA binding has recently been revealed from crystallography studies on the ARF1 and ARF5 DNA binding domains.
Golgi Fragmentation in ALS Motor Neurons. New Mechanisms Targeting Microtubules, Tethers, and Transport Vesicles.
Rabouille et al., Marseille, France. In Front Neurosci, 2014
These effects are partially rescued by the GTPase ARF1 through recruitment of TBCE to the Golgi.
Phospholipase D signaling pathways and phosphatidic acid as therapeutic targets in cancer.
Brown et al., Nashville, United States. In Pharmacol Rev, 2014
In mammalian cells, the pathways modulating catalytic activity involve a variety of cellular signaling components, including G protein-coupled receptors, receptor tyrosine kinases, polyphosphatidylinositol lipids, Ras/Rho/ADP-ribosylation factor GTPases, and conventional isoforms of protein kinase C, among others.
Structural basis for DNA binding specificity by the auxin-dependent ARF transcription factors.
Coll et al., Barcelona, Spain. In Cell, 2014
Here, we address this question by solving high-resolution crystal structures of the pivotal Arabidopsis developmental regulator ARF5/MONOPTEROS (MP), its divergent paralog ARF1, and a complex of ARF1 and a generic auxin response DNA element (AuxRE).
A CREB3-ARF4 signalling pathway mediates the response to Golgi stress and susceptibility to pathogens.
Sabatini et al., Cambridge, United States. In Nat Cell Biol, 2013
ARF4 depletion preserves viability, Golgi integrity and cargo trafficking in the presence of BFA, and these effects depend on the guanine nucleotide exchange factor GBF1 and other ARF isoforms including ARF1 and ARF5.
Proteolytic elimination of N-myristoyl modifications by the Shigella virulence factor IpaJ.
Alto et al., Dallas, United States. In Nature, 2013
A yeast genetic screen for IpaJ substrates identified ADP-ribosylation factor (ARF)1p and ARF2p, small molecular mass GTPases that regulate cargo transport through the Golgi apparatus.
Interleukin receptor activates a MYD88-ARNO-ARF6 cascade to disrupt vascular stability.
Li et al., Salt Lake City, United States. In Nature, 2013
Here we show that the direct, immediate and disruptive effects of IL-1β on endothelial stability in a human in vitro cell model are NF-κB independent and are instead the result of signalling through the small GTPase ADP-ribosylation factor 6 (ARF6) and its activator ARF nucleotide binding site opener (ARNO; also known as CYTH2).
ADP-ribosylation factor 1 protein regulates trypsinogen activation via organellar trafficking of procathepsin B protein and autophagic maturation in acute pancreatitis.
Singh et al., Pittsburgh, United States. In J Biol Chem, 2012
ARF1-dependent trafficking of procathepsin B and the maturation of autophagosomes results in cathepsin B-mediated trypsinogen activation induced by caerulein.
ARAP1 regulates the ring size of circular dorsal ruffles through Arf1 and Arf5.
Itoh et al., Kōbe, Japan. In Mol Biol Cell, 2012
a novel molecular mechanism of circular dorsal ruffles ring size control through the ARAP1-Arf1/5 pathway.
GBF1 bears a novel phosphatidylinositol-phosphate binding module, BP3K, to link PI3Kγ activity with Arf1 activation involved in GPCR-mediated neutrophil chemotaxis and superoxide production.
Sabe et al., Kumamoto, Japan. In Mol Biol Cell, 2012
GBF1-mediated Arf1 activation is necessary to unify cell polarity during chemotaxis
Overexpression of ADP-ribosylation factor 1 in human gastric carcinoma and its clinicopathological significance.
Lin et al., Taiwan. In Cancer Sci, 2012
ARF1-overexpressing clones display enhanced cell proliferation, migration, and invasion. Furthermore, ARF1-overexpression might contribute to poor prognosis of gastric carcinoma patients.
ARF1 and GBF1 generate a PI4P-enriched environment supportive of hepatitis C virus replication.
Chung et al., Beijing, China. In Plos One, 2011
the vesicular transport proteins ARF1 and GBF1 colocalized with PI4KIIIbeta and were both required for HCV replication
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