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ADP-ribosylation factor interacting protein 1

Arfaptin 1, Arfaptin
human homolog binds ADP-ribosylation factor (ARF) and inhibits ARF dependent phorbol ester induced secretion of matrix metalloproteinase 9 [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: p16, ARF1, ARF3, V1a, HAD
Papers on Arfaptin 1
Dimer of arfaptin 2 regulates NF-κB signaling by interacting with IKKβ/NEMO and inhibiting IKKβ kinase activity.
Hwang et al., Seoul, South Korea. In Cell Signal, Nov 2015
In this study, arfaptin 2 was identified as an IKKβ-specific binding partner.
Live-cell imaging of endogenous mRNAs with a small molecule.
Uesugi et al., Uji, Japan. In Angew Chem Int Ed Engl, Mar 2015
Application of the technology to mRNAs of a total of 84 human cytoskeletal genes allowed us to observe cellular dynamics of several endogenous mRNAs including arfaptin-2, cortactin, and cytoplasmic FMR1-interacting protein 2.
Arfaptin-1 negatively regulates Arl1-mediated retrograde transport.
Yu et al., Taiwan. In Plos One, 2014
In this study, we used differential affinity chromatography combined with mass spectrometry to identify Arf-interacting protein 1b (arfaptin-1b) as an Arl1-interacting protein and characterized a novel function for arfaptin-1 (including the arfaptin-1a and 1b isoforms) in Arl1-mediated retrograde transport.
Recruitment of arfaptins to the trans-Golgi network by PI(4)P and their involvement in cargo export.
Malhotra et al., Barcelona, Spain. In Embo J, 2013
The BAR (Bin/Amphiphysin/Rvs) domain proteins arfaptin1 and arfaptin2 are localized to the trans-Golgi network (TGN) and, by virtue of their ability to sense and/or generate membrane curvature, could play an important role in the biogenesis of transport carriers.
Inhibition of formyl peptide-stimulated phospholipase D activation by Fal-002-2 via blockade of the Arf6, RhoA and protein kinase C signaling pathways in rat neutrophils.
Wang et al., T'ai-chung-shih, Taiwan. In Naunyn Schmiedebergs Arch Pharmacol, 2013
Fal-002-2 also attenuated the membrane recruitment of Rho-associated protein kinase 1, phosphorylation of myosin light chain 2 at Thr18/Ser19 and PLD1 at Thr147, and the interaction of Arf6 with both arfaptin 1 and phosphatidylinositol 4-phosphate 5-kinase 1A.
Eisosome-driven plasma membrane organization is mediated by BAR domains.
Walther et al., Martinsried, Germany. In Nat Struct Mol Biol, 2011
Here we show that both proteins consist mostly of a banana-shaped BAR domain common to membrane sculpting proteins, most similar to the ones of amphiphysin, arfaptin 2 and endophilin 2. Our data reveal a previously unrecognized family of BAR-domain proteins involved in plasma membrane organization.
Arfaptins are localized to the trans-Golgi by interaction with Arl1, but not Arfs.
Shin et al., Kyoto, Japan. In J Biol Chem, 2011
Arfaptins (arfaptin-1 and arfaptin-2/POR1) were originally identified as binding partners of the Arf small GTPases.
Signaling mechanisms of inhibition of phospholipase D activation by CHS-111 in formyl peptide-stimulated neutrophils.
Wang et al., T'ai-chung-shih, Taiwan. In Biochem Pharmacol, 2011
CHS-111 reduced the cellular levels of GTP-bound RhoA, membrane recruitment of Rho-associated protein kinase 1 and the downstream myosin light chain 2 phosphorylation, and attenuated the interaction between phosphatidylinositol 4-phosphate 5-kinase (PIP5K) and Arf6, whereas it only slightly inhibited the guanine nucleotide exchange activity of human Dbs (DH/PH) protein and did not affect the arfaptin binding to Arf6.
PDZ domain protein-protein interactions: a case study with PICK1.
Dev, Basel, Switzerland. In Curr Top Med Chem, 2006
PICK1 is a 416 amino acid protein that contains a PDZ domain, a coiled-coil motif/arfaptin homology domain and an acidic c-terminal.
Phosphorylation of arfaptin 2 at Ser260 by Akt Inhibits PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment.
Humbert et al., Orsay, France. In J Biol Chem, 2005
We show that this survival effect involves the ADP-ribosylation factor-interacting protein arfaptin 2, the levels of which are increased in HD patients.
Assays and properties of arfaptin 2 binding to Rac1 and ADP-ribosylation factors (Arfs).
Exton et al., Dallas, United States. In Methods Enzymol, 2004
Arfaptin 1 and 2 were identified as targets for GTP bound ADP-ribosylation factors (Arfs).
Islet cell autoantigen of 69 kDa is an arfaptin-related protein associated with the Golgi complex of insulinoma INS-1 cells.
Solimena et al., Dresden, Germany. In J Biol Chem, 2003
ICA69 is therefore a novel arfaptin-related protein that is likely to play a role in membrane trafficking at the Golgi complex and immature secretory granules in neurosecretory cells.
Arfaptin 1 inhibits ADP-ribosylation factor-dependent matrix metalloproteinase-9 secretion induced by phorbol ester in HT 1080 fibrosarcoma cells.
Williger et al., Nashville, United States. In Febs Lett, 2003
inhibits ADP-ribosylation factor-dependent matrix metalloproteinase-9 secretion induced by phorbol ester in fibrosarcoma cells
Arfaptin 2 regulates the aggregation of mutant huntingtin protein.
D'Souza-Schorey et al., Amsterdam, Netherlands. In Nat Cell Biol, 2002
Here we demonstrate that expression of arfaptin 2/POR1 (partner of Rac1) in cultured cells induces the formation of pericentriolar and nuclear aggregates, which morphologically resemble mutant huntingtin aggregates characteristic of HD.
Regulation of Golgi structure and function by ARF-like protein 1 (Arl1).
Hong et al., Singapore, Singapore. In J Cell Sci, 2001
In addition, the GTP form of Arl1 interacts with arfaptin-2/POR1 but not GGA1, both of which interact with GTP-restricted ARF1, suggesting that Arl1 and ARF1 share some common effectors in regulating cellular events.
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