The Golgi is central for the modification and transport of proteins to their cellular destination. Its canonical structure in eukaryotes is that of stacked membranes, or cisternae. However, the Golgi structure is notably different in numerous parasitic groups and in budding yeast, which display a vesicular or tubular morphology. In their Research Article (Herman, Yiangou et al., 2018), Anastasios Tsaousis, Joel Dacks and colleagues set out to explore the Golgi in the free-living microbial amoeba Naegleria gruberi. The authors show an unstacked tubular membranous structure in cells, to which the N. gruberi homologue of the β-subunit of the COPI protein complex localises. The membranous structures are disrupted upon addition of Brefeldin A, which disassembles the Golgi complex. In addition, the authors identify several genes that encode Golgi-associated proteins in Naegleria species and confirm that they are expressed. This work provides the first direct evidence that there is a Golgi in Naegleria, and that it is present as tubular compartments. Thereby, the number of divergent Golgi morphologies observed has been extended. Golgi bodies are fragmented in numerous human pathologies, such as Alzheimer's and autoimmune diseases, which highlights the importance of understanding the evolution of the morphology of the Golgi.