title: 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.
authors.affiliation: Laboratory of Molecular Parasitology, Institute of Parasitology - University of Zurich, Winterthurerstrasse 266a, CH-8057 Zürich, Switzerland.
authors.forename: Jacqueline A
authors.initials: JA
authors.lastname: Ebneter
authors.affiliation: Laboratory of Molecular Parasitology, Institute of Parasitology - University of Zurich, Winterthurerstrasse 266a, CH-8057 Zürich, Switzerland. Electronic address: adrian.hehl@uzh.ch.
authors.forename: Adrian B
authors.initials: AB
authors.lastname: Hehl
mesh_terms: D033942:Adaptor Proteins, Vesicular Transport / Q000378:metabolism*; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism; D002966:Clathrin / Q000737:chemistry / Q000378:metabolism*; D016829:Giardia lamblia / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D054730:Protein Interaction Domains and Motifs; D053058:Trophozoites / Q000378:metabolism*
chemical_list: D033942:Adaptor Proteins, Vesicular Transport; D002966:Clathrin; C114154:epsin
keywords: Attachment; ENTH-domain; Epsin; Giardia; Lipid binding; Ventral disk