Structure of the STRA6 receptor for retinol uptake

Yunting Chen, Oliver B. Clarke, Jonathan Kim, Sean Stowe, Youn Kyung Kim, Zahra Assur, Michael Cavalier, Raquel Godoy-Ruiz, Desiree C. Von Alpen, Chiara Manzini, William S. Blaner, Joachim Frank, Loredana Quadro, David J. Weber, Lawrence Shapiro, Wayne A. Hendrickson, Filippo Mancia

Research output: Contribution to journalArticlepeer-review

55 Scopus citations


Vitamin A homeostasis is critical to normal cellular function. Retinol-binding protein (RBP) is the sole specific carrier in the bloodstream for hydrophobic retinol, the main form in which vitamin A is transported. The integral membrane receptor STRA6 mediates cellular uptake of vitamin A by recognizing RBP-retinol to trigger release and internalization of retinol.We present the structure of zebrafish STRA6 determined to 3.9-angstrom resolution by single-particle cryo-electron microscopy. STRA6 has one intramembrane and nine transmembrane helices in an intricate dimeric assembly. Unexpectedly, calmodulin is bound tightly to STRA6 in a noncanonical arrangement. Residues involved with RBP binding map to an archlike structure that covers a deep lipophilic cleft. This cleft is open to the membrane, suggesting a possible mode for internalization of retinol through direct diffusion into the lipid bilayer.

Original languageEnglish (US)
Article numberaad8266
Issue number6302
StatePublished - 2016

All Science Journal Classification (ASJC) codes

  • General

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