Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

A protocol for noninvasive quantification of dietary fat absorption in mice.

STAR protocols·2026
Same author

Pseudomonas hijacks lactate to rewire host defense.

American journal of respiratory cell and molecular biology·2026
Same author

Bile acids regulate lipid metabolism through selective actions on fatty acid absorption.

Cell metabolism·2025
Same author

A molecular tango between chromatin and metabolites orchestrates a feedback switch for alcohol consumption.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Pathways and Molecular Mechanisms Governing LDL Receptor Regulation.

Circulation research·2025
Same author

Alveolar macrophages: guardians of the alveolar lipid galaxy.

Current opinion in lipidology·2025

Related Experiment Video

Updated: Mar 20, 2026

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein
07:20

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein

Published on: June 16, 2023

2.9K

Intracellular Localization of Endogenous Mouse ABCG1 Is Mimicked by Both ABCG1-L550 and ABCG1-P550-Brief Report.

Elizabeth J Tarling1, Peter A Edwards2

  • 1From the Departments of Biological Chemistry (P.A.E.) and Medicine (E.J.T.), David Geffen School of Medicine at the University of California, Los Angeles. etarling@mednet.ucla.edu.

Arteriosclerosis, Thrombosis, and Vascular Biology
|May 28, 2016
PubMed
Summary

ATP-binding cassette transporter G1 (ABCG1) is an intracellular protein, not found on the plasma membrane. Both leucine and proline at position 550 variants mobilize cellular sterols effectively from the endoplasmic reticulum.

Keywords:
ABC transportercholesterol homeostasislipids

More Related Videos

Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells
08:02

Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells

Published on: October 17, 2025

1.1K
In Vivo Immunofluorescence Localization for Assessment of Therapeutic and Diagnostic Antibody Biodistribution in Cancer Research
08:53

In Vivo Immunofluorescence Localization for Assessment of Therapeutic and Diagnostic Antibody Biodistribution in Cancer Research

Published on: September 16, 2019

9.8K

Related Experiment Videos

Last Updated: Mar 20, 2026

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein
07:20

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein

Published on: June 16, 2023

2.9K
Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells
08:02

Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells

Published on: October 17, 2025

1.1K
In Vivo Immunofluorescence Localization for Assessment of Therapeutic and Diagnostic Antibody Biodistribution in Cancer Research
08:53

In Vivo Immunofluorescence Localization for Assessment of Therapeutic and Diagnostic Antibody Biodistribution in Cancer Research

Published on: September 16, 2019

9.8K

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Controversy exists regarding the subcellular localization of ATP-binding cassette transporter G1 (ABCG1).
  • Previous studies reported conflicting data on whether ABCG1 localizes to the plasma membrane or intracellular compartments.
  • The specific amino acid at position 550 (leucine vs. proline) was implicated in this localization difference.

Purpose of the Study:

  • To resolve conflicting reports on ABCG1 subcellular localization.
  • To investigate the functional significance of leucine or proline at amino acid position 550 of ABCG1.
  • To determine the precise cellular location and functional activity of ABCG1 variants.

Main Methods:

  • Transfection of multiple cell lines (CHO-K1, Cos-7, HEK293) with ABCG1 variants (L550 and P550).
  • Immunofluorescence studies to visualize ABCG1 localization.
  • Assessment of cholesterol efflux to high-density lipoprotein.
  • Measurement of sterol regulatory element-binding protein-2 activity.
  • Treatment of primary peritoneal macrophages with a liver X receptor agonist.

Main Results:

  • ABCG1 consistently localized to intracellular endosomal vesicles in all transfected cell lines, regardless of the amino acid at position 550.
  • Both ABCG1-L550 and ABCG1-P550 demonstrated equal efficacy in promoting cholesterol efflux.
  • Both variants were equally effective in inducing sterol regulatory element-binding protein-2 activity.
  • Endogenous ABCG1 in macrophages, upon LXR agonist treatment, localized to intracellular endosomes, not the plasma membrane.

Conclusions:

  • ABCG1 functions as an intracellular protein within the endosomal pathway.
  • The amino acid at position 550 (leucine or proline) does not alter ABCG1's intracellular localization or its sterol-mobilizing function.
  • ABCG1's role is to mobilize sterols from the endoplasmic reticulum for cellular efflux.