Secretory protein trafficking in Giardia intestinalis

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Abstract
Early diverged extant organisms, which may serve as convenient laboratory models to look for and study evolutionary ancient features of eukaryotic cell biology, are rare. The diplomonad Giardia intestinalis, a protozoan parasite known to cause diarrhoeal disease, has become an increasingly popular object of basic research in cell biology, not least because of a genome sequencing project nearing completion. Commensurate with its phylogenetic status, the Giardia trophozoite has a very basic secretory system and even lacks hallmark structures such as a morphologically identifiable Golgi apparatus. The cell's capacity for protein sorting is nevertheless unimpeded, exemplified by its ability to cope with massive amounts of newly synthesized cyst wall proteins and glycans, which are sorted to dedicated Golgi‐like compartments termed encystation‐specific vesicles (ESVs) generated from endoplasmic reticulum (ER)‐derived transport intermediates. This soluble bulk cargo is kept strictly separate from constitutively transported variant surface proteins during export, a function that is dependent on the stage‐specific recognition of trafficking signals. Encysting Giardia therefore provide a unique system for the study of unconventional, Golgi‐independent protein trafficking mechanisms in the broader context of eukaryotic endomembrane organization and evolution.