Open AccessThe ATP binding cassette transporter, ABCG1, localizes to cortical actin filaments
Author(s) -
Elvis Pandžić,
Ingrid C. Gelissen,
Renée Whan,
Philip J. Barter,
Dmitri Sviridov,
Katharina Gaus,
KerryAnne Rye,
Blake J. Cochran
Publication year - 2017
Publication title -
scientific reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.24
H-Index - 213
ISSN - 2045-2322
DOI - 10.1038/srep42025
Subject(s) - actin , transporter , microbiology and biotechnology , abcg1 , atp binding cassette transporter , chemistry , computational biology , biology , biochemistry , gene
The ATP-binding cassette sub-family G member 1 (ABCG1) exports cellular cholesterol to high-density lipoproteins (HDL). However, a number of recent studies have suggested ABCG1 is predominantly localised to intracellular membranes. In this study, we found that ABCG1 was organized into two distinct cellular pools: one at the plasma membrane and the other associated with the endoplasmic reticulum (ER). The plasma membrane fraction was organized into filamentous structures that were associated with cortical actin filaments. Inhibition of actin polymerization resulted in complete disruption of ABCG1 filaments. Cholesterol loading of the cells increased the formation of the filamentous ABCG1, the proximity of filamentous ABCG1 to actin filaments and the diffusion rate of membrane associated ABCG1. Our findings suggest that the actin cytoskeleton plays a critical role in the plasma membrane localization of ABCG1.