ArticleBiology open2015
The small G protein Arl5 contributes to endosome-to-Golgi traffic by aiding the recruitment of the GARP complex to the Golgi.
Article in Biology open, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- GARP Complex in Golgi Physiology.Sub-cellular biochemistry · 2026Review
- Endosomal traffic disorders: a driving force behind neurodegenerative diseases.Translational neurodegeneration · 2024Review
- ARMH3 is an ARL5 effector that promotes PI4KB-catalyzed PI4P synthesis at the trans-Golgi network.Nature communications · 2024Article
- Golgi-associated retrograde protein (GARP) complex-dependent endosomes to trans Golgi network retrograde trafficking is controlled by Rab4b.Cellular & molecular biology letters · 2024Article
- The Arf family GTPases: Regulation of vesicle biogenesis and beyond.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Review
- Role of GARP Vesicle Tethering Complex in Golgi Physiology.International journal of molecular sciences · 2023Review
- Defining the proximal interaction networks of Arf GTPases reveals a mechanism for the regulation of PLD1 and PI4KB.The EMBO journal · 2022Article
- Binding with heat shock cognate protein HSC70 fine-tunes the Golgi association of the small GTPase ARL5B.The Journal of biological chemistry · 2021Article
- The Golgi-associated retrograde protein (GARP) complex plays an essential role in the maintenance of the Golgi glycosylation machinery.Molecular biology of the cell · 2021Article
- Self-assemblies of Rab- and Arf-family small GTPases on lipid bilayers in membrane tethering.Biophysical reviews · 2021Review
- The Small GTPase Arf6 Functions as a Membrane Tether in a Chemically-Defined Reconstitution System.Frontiers in cell and developmental biology · 2021Article
- Ubiquitination-Dependent Regulation of Small GTPases in Membrane Trafficking: From Cell Biology to Human Diseases.Frontiers in cell and developmental biology · 2021Review
- MTV proteins unveil ER- and microtubule-associated compartments in the plant vacuolar trafficking pathway.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- ARFRP1 functions upstream of ARL1 and ARL5 to coordinate recruitment of distinct tethering factors to the trans-Golgi network.The Journal of cell biology · 2019Article
- ARF GTPases and their GEFs and GAPs: concepts and challenges.Molecular biology of the cell · 2019Review
- Amino acids stimulate the endosome-to-Golgi trafficking through Ragulator and small GTPase Arl5.Nature communications · 2018Article
- Retrograde Transport from Early Endosomes to the trans-Golgi Network Enables Membrane Wrapping and Egress of Vaccinia Virus Virions.Journal of virology · 2016Article
- The role of acroblast formation during Drosophila spermatogenesis.Biology open · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The small G proteins of the Arf family play critical roles in membrane trafficking and cytoskeleton organization. However, the function of some members of the family remains poorly understood including Arl5 which is widely conserved in eukaryotes. Humans have two closely related Arl5 paralogues (Arl5a and Arl5b), and both Arl5a and Arl5b localize to the trans-Golgi with Arl5b being involved in retrograde traffic from endosomes to the Golgi apparatus. To investigate the function of Arl5, we have used Drosophila melanogaster as a model system. We find that the single Arl5 orthologue in Drosophila also localizes to the trans-Golgi, but flies lacking the Arl5 gene are viable and fertile. By using both liposome and column based affinity chromatography methods we find that Arl5 interacts with the Golgi-associated retrograde protein (GARP) complex that acts in the tethering of vesicles moving from endosomes to the trans-Golgi network (TGN). In Drosophila tissues the GARP complex is partially displaced from the Golgi when Arl5 is absent, and the late endosomal compartment is enlarged. In addition, in HeLa cells GARP also becomes cytosolic upon depletion of Arl5b. These phenotypes are consistent with a role in endosome-to-Golgi traffic, but are less severe than loss of GARP itself. Thus it appears that Arl5 is one of the factors that directs the recruitment of the GARP complex to the trans-Golgi, and this function is conserved in both flies and humans.
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