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


Ebneter, Jacqueline A; Hehl, Adrian B (2014). The single epsin homolog in Giardia lamblia localizes to the ventral disk of trophozoites and is not associated with clathrin membrane coats. Molecular and Biochemical Parasitology, 197(1-2):24-27.

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.

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.

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Item Type:Journal Article, refereed, original work
Communities & Collections:05 Vetsuisse Faculty > Institute of Parasitology
04 Faculty of Medicine > Institute of Parasitology
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
600 Technology
Language:English
Date:October 2014
Deposited On:11 Feb 2015 10:29
Last Modified:14 Feb 2018 23:20
Publisher:Elsevier
ISSN:0166-6851
OA Status:Hybrid
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1016/j.molbiopara.2014.09.008
PubMed ID:25286382

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