ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Brown HA, Gutowski S, Moomaw CR, Slaughter C, Sternweis PC (1993) Cell 75: 1137-44 The proliferation gene expression signature is a quantitative integrator of oncogenic events that predicts survival in mantle cell lymphoma. Rosenwald A, Wright G, Wiestner A, Chan WC, Connors JM, Campo E, Gascoyne RD, Grogan TM, Muller-Hermelink HK, Smeland EB, Chiorazzi M, Giltnane JM, Hurt EM, Zhao H, Averett L, Henrickson S, Yang L, Powell J, Wilson WH, Jaffe ES, Simon R, Klausner RD, Montserrat E, Bosch F, Greiner TC, Weisenburger DD, Sanger WG, Dave BJ, Lynch JC, Vose J, Armitage JO, Fisher RI, Miller TP, LeBlanc M, Ott G, Kvaloy S, Holte H, Delabie J, Staudt LM (2003) Cancer Cell 3: 185-97 Novel role of ARF6 in vascular endothelial growth factor-induced signaling and angiogenesis. Ikeda S, Ushio-Fukai M, Zuo L, Tojo T, Dikalov S, Patrushev NA, Alexander RW (2005) Circ Res 96: 467-75 Evidence that phospholipase D mediates ADP ribosylation factor-dependent formation of Golgi coated vesicles. Ktistakis NT, Brown HA, Waters MG, Sternweis PC, Roth MG (1996) J Cell Biol 134: 295-306 Role for Drs2p, a P-type ATPase and potential aminophospholipid translocase, in yeast late Golgi function. Chen CY, Ingram MF, Rosal PH, Graham TR (1999) J Cell Biol 147: 1223-36 Nucleophosmin interacts directly with c-Myc and controls c-Myc-induced hyperproliferation and transformation. Li Z, Boone D, Hann SR (2008) Proc Natl Acad Sci U S A 105: 18794-9 Phospholipase D is present on Golgi-enriched membranes and its activation by ADP ribosylation factor is sensitive to brefeldin A. Ktistakis NT, Brown HA, Sternweis PC, Roth MG (1995) Proc Natl Acad Sci U S A 92: 4952-6 Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1. Betz SF, Schnuchel A, Wang H, Olejniczak ET, Meadows RP, Lipsky BP, Harris EA, Staunton DE, Fesik SW (1998) Proc Natl Acad Sci U S A 95: 7909-14 The ADP ribosylation factor nucleotide exchange factor ARNO promotes beta-arrestin release necessary for luteinizing hormone/choriogonadotropin receptor desensitization. Mukherjee S, Gurevich VV, Jones JC, Casanova JE, Frank SR, Maizels ET, Bader MF, Kahn RA, Palczewski K, Aktories K, Hunzicker-Dunn M (2000) Proc Natl Acad Sci U S A 97: 5901-6 Arl1 gets into the membrane remodeling business with a flippase and ArfGEF. Graham TR (2013) Proc Natl Acad Sci U S A 110: 2691-2 Egr1 mediates p53-independent c-Myc-induced apoptosis via a noncanonical ARF-dependent transcriptional mechanism. Boone DN, Qi Y, Li Z, Hann SR (2011) Proc Natl Acad Sci U S A 108: 632-7 Membrane targeting: getting Arl to the Golgi. Graham TR (2004) Curr Biol 14: R483-5 Loss of one allele of ARF rescues Mdm2 haploinsufficiency effects on apoptosis and lymphoma development. Eischen CM, Alt JR, Wang P (2004) Oncogene 23: 8931-40 Neurotrophin Responsiveness of Sympathetic Neurons Is Regulated by Rapid Mobilization of the p75 Receptor to the Cell Surface through TrkA Activation of Arf6. Hickman FE, Stanley EM, Carter BD (2018) J Neurosci 38: 5606-5619 ATF6 activation reduces the secretion and extracellular aggregation of destabilized variants of an amyloidogenic protein. Chen JJ, Genereux JC, Qu S, Hulleman JD, Shoulders MD, Wiseman RL (2014) Chem Biol 21: 1564-74 Apoptosis triggered by Myc-induced suppression of Bcl-X(L) or Bcl-2 is bypassed during lymphomagenesis. Eischen CM, Woo D, Roussel MF, Cleveland JL (2001) Mol Cell Biol 21: 5063-70 Aspartic acid 564 in the third cytoplasmic loop of the luteinizing hormone/choriogonadotropin receptor is crucial for phosphorylation-independent interaction with arrestin2. Mukherjee S, Gurevich VV, Preninger A, Hamm HE, Bader MF, Fazleabas AT, Birnbaumer L, Hunzicker-Dunn M (2002) J Biol Chem 277: 17916-27 Regulation of GRP1-catalyzed ADP ribosylation factor guanine nucleotide exchange by phosphatidylinositol 3,4,5-trisphosphate. Klarlund JK, Rameh LE, Cantley LC, Buxton JM, Holik JJ, Sakelis C, Patki V, Corvera S, Czech MP (1998) J Biol Chem 273: 1859-62 Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity. Singer WD, Brown HA, Jiang X, Sternweis PC (1996) J Biol Chem 271: 4504-10 Kinetic analysis of a mammalian phospholipase D: allosteric modulation by monomeric GTPases, protein kinase C, and polyphosphoinositides. Henage LG, Exton JH, Brown HA (2006) J Biol Chem 281: 3408-17 Partial purification and characterization of Arf-sensitive phospholipase D from porcine brain. Brown HA, Gutowski S, Kahn RA, Sternweis PC (1995) J Biol Chem 270: 14935-43 Resolved phospholipase D activity is modulated by cytosolic factors other than Arf. Singer WD, Brown HA, Bokoch GM, Sternweis PC (1995) J Biol Chem 270: 14944-50 An arf1Delta synthetic lethal screen identifies a new clathrin heavy chain conditional allele that perturbs vacuolar protein transport in Saccharomyces cerevisiae. Chen CY, Graham TR (1998) Genetics 150: 577-89 RABL6A, a novel RAB-like protein, controls centrosome amplification and chromosome instability in primary fibroblasts. Zhang X, Hagen J, Muniz VP, Smith T, Coombs GS, Eischen CM, Mackie DI, Roman DL, Van Rheeden R, Darbro B, Tompkins VS, Quelle DE (2013) PLoS One 8: e80228 ADP ribosylation factor 6 binding to phosphatidylinositol 4,5-bisphosphate-containing vesicles creates defects in the bilayer structure: an electron spin resonance study. Ge M, Cohen JS, Brown HA, Freed JH (2001) Biophys J 81: 994-1005 Ordered and disordered phases coexist in plasma membrane vesicles of RBL-2H3 mast cells. An ESR study. Ge M, Gidwani A, Brown HA, Holowka D, Baird B, Freed JH (2003) Biophys J 85: 1278-88 ARF6: a newly appreciated player in G protein-coupled receptor desensitization. Hunzicker-Dunn M, Gurevich VV, Casanova JE, Mukherjee S (2002) FEBS Lett 521: 3-8 Stimulation of phospholipase D by ADP-ribosylation factor. Brown HA, Sternweis PC (1995) Methods Enzymol 257: 313-24
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