| C9orf72 Toxic Species Affect ArfGAP-1 Function. | C9orf72 Toxic Species Affect ArfGAP-1 Function.
Rossi S, Di Salvio M, Balì M, De Simone A, Apolloni S, D'Ambrosi N, Arisi I, Cipressa F, Cozzolino M, Cestra G., Free PMC Article | 08/14/2023 |
| ArfGAP1 inhibits mTORC1 lysosomal localization and activation. | ArfGAP1 inhibits mTORC1 lysosomal localization and activation.
Meng D, Yang Q, Melick CH, Park BC, Hsieh TS, Curukovic A, Jeong MH, Zhang J, James NG, Jewell JL., Free PMC Article | 11/13/2021 |
| ArfGAP1 acts as a GTPase-activating protein for human ADP-ribosylation factor-like 1 protein. | ArfGAP1 acts as a GTPase-activating protein for human ADP-ribosylation factor-like 1 protein.
Feng HP, Cheng HY, Hsiao TF, Lin TW, Hsu JW, Huang LH, Yu CJ. | 07/24/2021 |
| ArfGAP1 restricts Mycobacterium tuberculosis entry by controlling the actin cytoskeleton. | ArfGAP1 restricts Mycobacterium tuberculosis entry by controlling the actin cytoskeleton.
Song OR, Queval CJ, Iantomasi R, Delorme V, Marion S, Veyron-Churlet R, Werkmeister E, Popoff M, Ricard I, Jouny S, Deboosere N, Lafont F, Baulard A, Yeramian E, Marsollier L, Hoffmann E, Brodin P., Free PMC Article | 01/5/2019 |
| ARFGAP1 is found associated with lipid droplets at steady state in some but not all hepatocytes. | ARFGAP1 is dynamically associated with lipid droplets in hepatocytes.
Gannon J, Fernandez-Rodriguez J, Alamri H, Feng SB, Kalantari F, Negi S, Wong AH, Mazur A, Asp L, Fazel A, Salman A, Lazaris A, Metrakos P, Bergeron JJ, Nilsson T., Free PMC Article | 07/25/2015 |
| ARFGAP1 is a host factor for Hepatitis C Virus RNA replication, and is hijacked by HCV NS5A to remove COPI cargo Sac1 from the site of HCV replication to maintain high levels of PI4P. | Hepatitis C virus NS5A hijacks ARFGAP1 to maintain a phosphatidylinositol 4-phosphate-enriched microenvironment.
Li H, Yang X, Yang G, Hong Z, Zhou L, Yin P, Xiao Y, Chen L, Chung RT, Zhang L., Free PMC Article | 07/5/2014 |
| ArfGAP1 is identified as the first GTPase activating protein (GAP) for leucine-rich repeat kinase 2 (LRRK2). | ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2.
Xiong Y, Yuan C, Chen R, Dawson TM, Dawson VL., Free PMC Article | 05/5/2012 |
| role of ARFGAP1 in AP-2-regulated endocytosis has mechanistic parallels with its roles in COPI transport, as both its GAP activity and coat function contribute to promoting AP-2 transport | ARFGAP1 promotes AP-2-dependent endocytosis.
Bai M, Gad H, Turacchio G, Cocucci E, Yang JS, Li J, Beznoussenko GV, Nie Z, Luo R, Fu L, Collawn JF, Kirchhausen T, Luini A, Hsu VW., Free PMC Article | 07/16/2011 |
| ArfGAP1, ArfGAP2, and ArfGAP3 have overlapping roles in regulating COPI function in Golgi-to-ER retrograde transport. | Three homologous ArfGAPs participate in coat protein I-mediated transport.
Saitoh A, Shin HW, Yamada A, Waguri S, Nakayama K., Free PMC Article | 01/21/2010 |
| catalytic amounts of Arf1GAP1 significantly reduce the yield of purified COPI vesicles | ArfGAP1 activity and COPI vesicle biogenesis.
Beck R, Adolf F, Weimer C, Bruegger B, Wieland FT. | 01/21/2010 |
| Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI trafficking | Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI trafficking.
Weimer C, Beck R, Eckert P, Reckmann I, Moelleken J, Brügger B, Wieland F., Free PMC Article | 01/21/2010 |
| coatomer is an allosteric regulator of Arf GAP1 | Kinetic analysis of Arf GAP1 indicates a regulatory role for coatomer.
Luo R, Randazzo PA., Free PMC Article | 01/21/2010 |
| The small GTPases of the Ras superfamily mediate numerous biological processes through their ability to cycle between an inactive GDP-bound and an active GTP-bound form. | GAP control: regulating the regulators of small GTPases.
Bernards A, Settleman J. | 01/21/2010 |
| ArfGAP1 interacts with the Golgi through multiple hydrophobic motifs and that alternative modes of interaction may exist in tissue-specific ArfGAP1 isoforms. | Golgi localization determinants in ArfGAP1 and in new tissue-specific ArfGAP1 isoforms.
Parnis A, Rawet M, Regev L, Barkan B, Rotman M, Gaitner M, Cassel D. | 01/21/2010 |
| SMAP2 functions in the retrograde, early endosome-to-trans golig network pathway in a clathrin- and AP-1-dependent manner. | SMAP2, a novel ARF GTPase-activating protein, interacts with clathrin and clathrin assembly protein and functions on the AP-1-positive early endosome/trans-Golgi network.
Natsume W, Tanabe K, Kon S, Yoshida N, Watanabe T, Torii T, Satake M., Free PMC Article | 01/21/2010 |