A membrane receptor for retinol binding protein mediates cellular uptake of vitamin A

Science. 2007 Feb 9;315(5813):820-5. doi: 10.1126/science.1136244. Epub 2007 Jan 25.


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. We identified in bovine retinal pigment epithelium cells 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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / metabolism
  • Amino Acid Sequence
  • Animals
  • Blood-Retinal Barrier
  • COS Cells
  • Cattle
  • Cell Line
  • Cell Line, Tumor
  • Cell Membrane / metabolism
  • Chlorocebus aethiops
  • Embryonic Development
  • Endocytosis
  • Humans
  • Molecular Sequence Data
  • Mutation, Missense
  • Pigment Epithelium of Eye / metabolism*
  • Placenta / metabolism
  • Receptors, Cell Surface / metabolism*
  • Retinal Vessels / metabolism
  • Retinol-Binding Proteins / metabolism*
  • Spleen / metabolism
  • Transfection
  • Vitamin A / metabolism*


  • Receptors, Cell Surface
  • Retinol-Binding Proteins
  • retinol binding protein receptor
  • Vitamin A
  • Acyltransferases
  • lecithin-retinol acyltransferase