Arl1 gets into the membrane remodeling business with a flippase and ArfGEF

Graham, Todd R.

doi:10.1073/pnas.1300420110

Cited by 4 publications

(5 citation statements)

References 13 publications

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“…Indeed, activated Arl1 interacts with the flippase Drs2 within the context of a ternary complex with Gea2, which is important for lipid asymmetry and Arl1 function at the Golgi (Tsai et al, 2013). This raises the question of why the activity of the Golgi phospholipid flippase needs to be regulated in a complex formed with proteins that have other functions (Graham, 2013). Another question is whether Gea2 is also capable of activating Arf as part of the Arl1-Gea2-Drs2 complex, or whether these two activities are mutually exclusive.…”

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Multiple activities of Arl1 GTPase in the trans-Golgi network

Lee

2017

Journal of Cell Science

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ADP-ribosylation factors (Arfs) and ADP-ribosylation factor-like proteins (Arls) are highly conserved small GTPases that function as main regulators of vesicular trafficking and cytoskeletal reorganization. Arl1, the first identified member of the large Arl family, is an important regulator of Golgi complex structure and function in organisms ranging from yeast to mammals. Together with its effectors, Arl1 has been shown to be involved in several cellular processes, including endosomal trans-Golgi network and secretory trafficking, lipid droplet and salivary granule formation, innate immunity and neuronal development, stress tolerance, as well as the response of the unfolded protein. In this Commentary, we provide a comprehensive summary of the Arl1-dependent cellular functions and a detailed characterization of several Arl1 effectors. We propose that involvement of Arl1 in these diverse cellular functions reflects the fact that Arl1 is activated at several late-Golgi sites, corresponding to specific molecular complexes that respond to and integrate multiple signals. We also provide insight into how the GTP-GDP cycle of Arl1 is regulated, and highlight a newly discovered mechanism that controls the sophisticated regulation of Arl1 activity at the Golgi complex.

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Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Multiple activities of Arl1 GTPase in the trans-Golgi network

Lee

2017

Journal of Cell Science

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“…reported a unique function for Arl1p in membrane remodeling, in which activated Arl1p promotes the spatial modulation of membrane organization at the TGN through interactions with Arf-GEF Gea2p and the flippase Drs2p. That study also showed that the Arl1p-Drs2p-Gea2p complex is specifically required for recruiting the GRIP domain-containing protein Imh1p to the Golgi [ 30 , 31 ]. These studies suggest that Arl1, together with its effectors and a flippase, induces membrane curvature at the TGN, providing a platform for coat protein, coat accessory protein or tethering protein binding, and regulating the retrieval of selected cargo proteins from endosomes to the TGN.…”

Section: Discussionmentioning

confidence: 99%

Arfaptin-1 Negatively Regulates Arl1-Mediated Retrograde Transport

et al. 2015

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The small GTPase Arf-like protein 1 (Arl1) is well known for its role in intracellular vesicular transport at the trans-Golgi network (TGN). 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. Using a Shiga-toxin subunit B (STxB) transportation assay, we demonstrated that knockdown of arfaptin-1 accelerated the retrograde transport of STxB from the endosome to the Golgi apparatus, whereas Arl1 knockdown inhibited STxB transport compared with control cells. Arfaptin-1 overexpression, but not an Arl1 binding-defective mutant (arfaptin-1b-F317A), consistently inhibited STxB transport. Exogenous arfaptin-1 expression did not interfere with the localization of the Arl1-interacting proteins golgin-97 and golgin-245 to the TGN and vice versa. Moreover, we found that the N-terminal region of arfaptin-1 was involved in the regulation of retrograde transport. Our results show that arfaptin-1 acts as a negative regulator in Arl1-mediated retrograde transport and suggest that different functional complexes containing Arl1 form in distinct microdomains and are responsible for different functions.

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“…ARL1 is found at the Golgi complex and its active conformation recruits various effectors to the Golgi, especially GRIPdomain-containing coiled-coil proteins. Depletion of mammalian ARL1 results in defective protein transport between endosomes and the Golgi complex, but its precise role is unknown (Lu et al 2005;Graham 2013).…”

Section: Arl1-arl3mentioning

confidence: 99%

The Function of Arf-like Proteins ARL2 and ARL3 in Photoreceptors

Hanke-Gogokhia

Zhang

Frederick

et al. 2015

Advances in Experimental Medicine and Biology

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Arf-like proteins (ARLs) are ubiquitously expressed small G proteins of the RAS superfamily. In photoreceptors, ARL2 and ARL3 participate in the trafficking of lipidated membrane-associated proteins and colocalize in the inner segment with UNC119A and PDEδ. UNC119A and PDEδ are acyl- and prenyl-binding proteins, respectively, involved in trafficking of acylated (transducin-α subunit, nephrocystin NPHP3) and prenylated proteins (GRK1, PDE6). Germline Arl3 knockout mice do not survive beyond postnatal day 21 and display ciliary defects in multiple organs (kidney, liver and pancreas) as well as retinal degeneration. Conditional knockouts will be necessary to delineate mechanisms of protein transport in retina disease.

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Arl1 gets into the membrane remodeling business with a flippase and ArfGEF

Cited by 4 publications

References 13 publications

Multiple activities of Arl1 GTPase in the trans-Golgi network

Multiple activities of Arl1 GTPase in the trans-Golgi network

Arfaptin-1 Negatively Regulates Arl1-Mediated Retrograde Transport

The Function of Arf-like Proteins ARL2 and ARL3 in Photoreceptors

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