| 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 |
| The ARFRP1 functions upstream of two other ARL GTPases, ARL1 and ARL5, which in turn recruit golgins and GARP, respectively, to the trans-Golgi network (TGN). | ARFRP1 functions upstream of ARL1 and ARL5 to coordinate recruitment of distinct tethering factors to the trans-Golgi network.
Ishida M, Bonifacino JS., Free PMC Article | 05/16/2020 |
| Plasticity allows Arl1 to interact with different effectors of unrelated structure. | Structural Insights into Arl1-Mediated Targeting of the Arf-GEF BIG1 to the trans-Golgi.
Galindo A, Soler N, McLaughlin SH, Yu M, Williams RL, Munro S., Free PMC Article | 11/26/2017 |
| Together the findings indicate that Arl1 links Rab4-dependent formation of endosomal sorting domains with downstream assembly of adaptor protein complexes that constitute the endosomal sorting machinery. | Rab4 orchestrates a small GTPase cascade for recruitment of adaptor proteins to early endosomes.
D'Souza RS, Semus R, Billings EA, Meyer CB, Conger K, Casanova JE., Free PMC Article | 09/26/2015 |
| results demonstrate that activated Arl1p can promote the spatial modulation of membrane organization at the trans-Golgi network through interacting with the effectors Gea2p and Drs2p | Arl1p regulates spatial membrane organization at the trans-Golgi network through interaction with Arf-GEF Gea2p and flippase Drs2p.
Tsai PC, Hsu JW, Liu YW, Chen KY, Lee FJ., Free PMC Article | 04/27/2013 |
| The Arl1.Arfaptin-2 BAR structure suggests that one of the two Arl1 molecules competes with Rac1, which binds to the concave face of the Arfaptin-2 BAR homodimer and may hinder its membrane association. | Structural basis for membrane binding specificity of the Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-2 determined by Arl1 GTPase.
Nakamura K, Man Z, Xie Y, Hanai A, Makyio H, Kawasaki M, Kato R, Shin HW, Nakayama K, Wakatsuki S., Free PMC Article | 10/20/2012 |
| arfaptins are recruited onto trans-Golgi membranes by interacting with Arl1, and capable of inducing membrane deformation via their BAR domains. | Arfaptins are localized to the trans-Golgi by interaction with Arl1, but not Arfs.
Man Z, Kondo Y, Koga H, Umino H, Nakayama K, Shin HW., Free PMC Article | 06/4/2011 |
| Study demonstrates that Golgi recruitment of endogenous GCC185 does not involve Rab6A/A' and Arl1. | The localization of the Golgin GCC185 is independent of Rab6A/A' and Arl1.
Houghton FJ, Chew PL, Lodeho S, Goud B, Gleeson PA. | 01/21/2010 |
| Results show that ARL1 and ARFRP1 regulate retrograde transport of Shiga toxin to the TGN and anterograde transport of VSVG from the TGN, respectively. | Differential effects of depletion of ARL1 and ARFRP1 on membrane trafficking between the trans-Golgi network and endosomes.
Nishimoto-Morita K, Shin HW, Mitsuhashi H, Kitamura M, Zhang Q, Johannes L, Nakayama K., Free PMC Article | 01/21/2010 |
| Data show that Arl1 regulates the membrane recruitment of Golgin-97, which plays a role in transport from the endosome to the trans-Golgi network. | Autoantigen Golgin-97, an effector of Arl1 GTPase, participates in traffic from the endosome to the trans-golgi network.
Lu L, Tai G, Hong W., Free PMC Article | 01/21/2010 |
| These data suggest that lethality of Arfrp1 knockout embryos is due to a specific disruption of protein targeting, e.g., of ARL1 and Golgin-245, to the Golgi. | Knockout of Arfrp1 leads to disruption of ARF-like1 (ARL1) targeting to the trans-Golgi in mouse embryos and HeLa cells.
Zahn C, Hommel A, Lu L, Hong W, Walther DJ, Florian S, Joost HG, Schürmann A. | 01/21/2010 |