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Published Online January 25, 2007
Science DOI: 10.1126/science.1136244

Research Articles

Submitted on October 12, 2006
Accepted on December 5, 2006

A Membrane Receptor for Retinol Binding Protein Mediates Cellular Uptake of Vitamin A

Riki Kawaguchi 1, Jiamei Yu 2, Jane Honda 2, Jane Hu 3, Julian Whitelegge 4, Peipei Ping 5, Patrick Wiita 2, Dean Bok 6, Hui Sun 7*

1 Department of Physiology; Jules Stein Eye Institute
2 Department of Physiology
3 Jules Stein Eye Institute
4 Pasarow Mass Spectrometry Laboratory, Semel Institute; Brain Research Institute
5 Department of Physiology; Department of Medicine
6 Jules Stein Eye Institute; Brain Research Institute; Department of Neurobiology, David Geffen School of Medicine at UCLA, 650 Charles E. Young Drive South, Los Angeles, CA 90095-1751, U.S.A.
7 Department of Physiology; Jules Stein Eye Institute; Brain Research Institute

* To whom correspondence should be addressed.
Hui Sun , E-mail: hsun{at}mednet.ucla.edu

Vitamin A has diverse biological functions. It is transported in the blood as a complex with retinol binding protein (RBP), but the molecular mechanism by which vitamin A is absorbed by cells from the vitamin A-RBP complex is not clearly understood. Here, we identified STRA6, a multitransmembrane domain protein, as a specific membrane receptor for RBP. STRA6 binds to RBP with high affinity and has robust vitamin A uptake activity from the vitamin A-RBP complex. It is widely expressed in embryonic development and in adult organ systems. The RBP receptor represents a major physiological mediator of cellular vitamin A uptake.


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