Advanced search×

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

Riki Kawaguchi, Jiamei Yu, Jane Honda, Jane Hu, Julian Whitelegge, Peipei Ping, Patrick Wiita, Dean Bok, and Hui Sun

Science 315(5813):820-5 (2007) PMID 17255476

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.

DOI: 10.1126/science.1136244
Version: za2963e q8za1 q8zbd q8zc7 q8zd6 q8zeb q8zf5 q8zgd
Buy PDF

Similar articles you may find interesting…

  1. Selective binding of antimicrobial porphyrins to the heme-receptor IsdH-NEAT3 of staphylococcus aureus.
    Nhuan T Vu, Yoshitaka Moriwaki, and Kouhei Tsumoto

    Protein Sci (2013) PMID 23649633

    We recently reported that the extracellular heme receptor IsdH-NEAT3 captures and transfers non-iron antimicrobial porphyrins containing metals in oxidation state (III). However, it is unclear if geometric factors such as the size of the metal (ionic radius) affect binding and transfer of metallopor...
    Buy PDF
  2. Avicularin, a plant flavonoid, suppresses lipid accumulation through repression of C/EBPα-activated GLUT4-mediated glucose uptake in 3T3-L1 ...
    Ko Fujimori and Makio Shibano

    J Agric Food Chem (2013) PMID 23647459

    We found that avicularin suppressed the accumulation of intracellular lipids through repression of glucose transporter 4 (GLUT4)-mediated glucose uptake in mouse adipocytic 3T3-L1 cells. Avicularin was highly purified (purity of more than at least 99%) from Taxillus kaempferi (DC.) Danser (Loranthac...
    Buy PDF
  3. Protein fishing using magnetic nano-beads containing calmodulin site-specifically immobilized via an azido-group.
    Akiyoshi Ikeda-Boku, Keisuke Kondo, and Kazuya Nishikawa

    J Biol Chem (2013) PMID 23653405

    We developed a novel method for capturing proteins which interact with a target protein. This method utilizes a protein containing a site-specifically incorporated 3-azidotyrosine (N3-Y) and FG beads for immobilization of the protein via the azido group. Using calmodulin (CaM) as the target protein,...
    PDF not found