Structure of the STRA6 receptor for retinol uptake

Author:

Chen Yunting1,Clarke Oliver B.2,Kim Jonathan1,Stowe Sean3,Kim Youn-Kyung4,Assur Zahra1,Cavalier Michael3,Godoy-Ruiz Raquel3,von Alpen Desiree C.5,Manzini Chiara5,Blaner William S.6,Frank Joachim2,Quadro Loredana4,Weber David J.3,Shapiro Lawrence2,Hendrickson Wayne A.12,Mancia Filippo1

Affiliation:

1. Department of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA.

2. Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.

3. The Center for Biomolecular Therapeutics and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.

4. Department of Food Science and Rutgers Center for Lipid Research, Rutgers University, New Brunswick, NJ 08901, USA.

5. Department of Pharmacology and Physiology and Department of Integrative Systems Biology, George Washington University, Washington, DC 20037, USA.

6. Department of Medicine, Columbia University, New York, NY 10032, USA.

Abstract

A window into the cell for vitamin A Vitamin A is an essential nutrient for mammals, and its metabolites affect diverse biological processes. It is carried in the bloodstream as retinol by retinol binding protein (RBP); a protein called STRA6 is implicated in facilitating retinol translocation across the cell membrane. Chen et al. determined the structure of zebrafish STRA6 to a resolution of 3.9 Å by electron microscopy. A lipophilic cleft is a likely binding site for RBP, and an opening in the cleft may allow retinol to diffuse into the membrane. Unexpectedly, the structure also includes bound calcium-modulated protein, but its function remains unclear. Science , this issue p. 887

Funder

NIH National Institute of General Medical Sciences

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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