Abstract
Protein recycling is important for maintaining homeostasis of the Golgi and its cisternae. The Vps54 (Scat) protein, a subunit of the GARP tethering complex, is a central factor in retrograde transport to the trans-Golgi. We found the scat(1) mutant to be male sterile in Drosophila with individualization problems occurring during spermatogenesis. Another typically observed phenotype was the abnormal nuclear structure in elongated mutant cysts. When examining the structure and function of the Golgi, a failure in acrosome formation and endosome-Golgi vesicular transport were found in the scat(1) mutant. This acrosome formation defect was due to a fault in the trans-Golgi side of the acroblast ribbon. When testing a mutation in a second retrograde transport protein, Fws, a subunit of the conserved oligomeric Golgi (COG) tethering complex, the acroblast structure, was again disrupted. fws(P) caused a similar, albeit milder, acrosome and sperm individualization phenotype as the scat(1) mutant. In the case of fws(P) the cis side of the acroblast ribbon was dispersed, in-line with the intra-Golgi retrograde function of COG. Our results highlight the importance of an intact acroblast for acrosome formation, nuclear elongation and therefore sperm maturation. Moreover, these results suggest the importance of retrograde tethering complexes in the formation of a functional Golgi ribbon.
