The single epsin homolog in Giardia lamblia localizes to the ventral disk of trophozoites and is not associated with clathrin membrane coats

Abstract

Epsins serve as recruitment platforms for clathrin membrane coat protein components and induce membrane curvature via their N-terminal homology (ENTH) domain. Unexpectedly, the single ENTH domain protein, a putative epsinR homolog (Glepsin), in the diverged protozoan parasite Giardia lamblia, localizes exclusively to the specialized attachment organelle, the ventral disk (VD). Glepsin binds both to phosphatidylinositol (3,4,5)-trisphosphate phospholipids and the VD cytoskeleton, but lacks canonical domains for interaction with clathrin coat components. This suggests reassignment of giardial epsin function from membrane trafficking to a structural role in linking the plasma membrane to the highly specialized VD during evolution of this genus.