Vacuolar protein sorting mechanisms in apicomplexan parasites

Mol Biochem Parasitol. 2016 Feb 1. pii: S0166-6851(16)30007-X. doi: 10.1016/j.molbiopara.2016.01.007. [Epub ahead of print]

Jimenez-Ruiz E¹, Morlon-Guyot J², Daher W³, Meissner M⁴.

The phylum Apicomplexa comprises more than 5000 species including pathogens of clinical and economical importance. These obligate intracellular parasites possess a highly complex endomembrane system to build among others three morphologically distinct secretory organelles: rhoptries, micronemes and dense granules. Proteins released by these organelles are essential for invasion and hijacking of the host cell. Due to the complexity of the internal organization of these parasites, a wide panoply of trafficking factors was expected to be required for the correct sorting of proteins towards the various organelles. However, T. gondii and other apicomplexan parasites contain only a core set of these factors and several of the vacuolar protein sorting (VPS) homologs found in most eukaryotes have been lost in this phylum. In this review, we will summarise our current knowledge about the role of trafficking complexes in Toxoplasma gondii, highlighting recent studies focused on complexes formed by VPS proteins. We also present a novel, hypothetical model, suggesting the recycling of parasite membrane and micronemal proteins.
Copyright © 2016. Published by Elsevier B.V.

KEYWORDS:

Multi-subunit tethering complex; Toxoplasma gondii; microneme recycling; vesicular protein sorting

PMID:

26844642

[PubMed - as supplied by publisher]