From all to (nearly) none

The five adaptor protein (AP) complexes function in cargo-selection and coat-recruitment stages of vesicular transport in eukaryotic cells. Much of what we know about AP complex function has come from experimental work using Saccharomyces cerevisiae as a model. Here, using a combination of comparative genomic and phylogenetic approaches we provide evolutionary context for the knowledge gained from this model system by searching the genomes of diverse fungi as well as a member of the sister group to all fungi, Fonticula alba, for presence of AP subunits. First, we demonstrate that F. alba contains all five AP complexes; whereas, similar to S. cerevisiae, most fungi retain only AP-1 to 3. As exceptions, the glomeromycete Rhizophagus irregularis maintains a complete AP-4 and chytrid fungi Spizellomyces punctatus and Batrachochytrium dendrobatidis retain partial AP-4 complexes. The presence of AP-4 subunits in diverse fungi suggests that AP-4 has been independently lost up to seven times in the fungal lineage. In addition to the trend of loss in fungi, we demonstrate that the duplication that gave rise to the β subunits of the AP-1 and AP-2 complexes in S. cerevisiae occurred before the divergence of F. alba and Fungi. Finally, our investigation into the AP complement of basal fungi (Microsporidia and Cryptomycota) demonstrates that while the cryptomycete Rozella allomyces contains an adaptin complement similar to other fungi, the extremely reduced Microsporidia retain, at most, a single cryptic AP complex in the absence of clathrin or any other putative AP-associated coat protein.