Cross Talk between Signaling and Vitamin A Transport by the Retinol-Binding Protein Receptor STRA6

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Published inMolecular and Cellular Biology Vol. 32; no. 15; pp. 3164 - 3175
Main Authors Berry, Daniel C., O'Byrne, Sheila M., Vreeland, Amanda C., Blaner, William S., Noy, Noa
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.08.2012
Taylor & Francis
Subjects
3T3 Cells
Animals
Biological Transport, Active
Cell Line, Tumor
Cell Physiological Phenomena
Hep G2 Cells
Humans
Male
Membrane Proteins - metabolism
Mice
Receptors, Cell Surface - metabolism
Retinol-Binding Proteins - metabolism
Signal Transduction
Vitamin A - metabolism
Online AccessGet full text

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Abstract Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
AbstractList The plasma membrane protein STRA6 transports vitamin A from its blood carrier retinol binding protein (RBP) into cells, and it also functions as a cytokine receptor which activates JAK/STAT signaling. We show here that, unlike other cytokine receptors, phosphorylation of STRA6 is not simply induced upon binding of its extracellular ligand. Instead, activation of the receptor is triggered by STRA6-mediated translocation of retinol from serum RBP to an intracellular acceptor, the retinol-binding protein CRBP-I. The observations also demonstrate that the movement of retinol from RBP to CRBP-I, and thus activation of STRA6, is critically linked to the intracellular metabolism of the vitamin. Furthermore, the data show that STRA6 phosphorylation is required for retinol uptake to proceed. Hence, the observations demonstrate that STRA6 orchestrates a multicomponent "machinery" that couples vitamin A homeostasis and metabolism to activation of a signaling cascade and that, in turn, STRA6 signaling regulates the cellular uptake of the vitamin. STRA6 appears to be a founding member of a new class of proteins that may be termed "cytokine signaling transporters."
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Author Sheila M. O'Byrne
Daniel C. Berry
Amanda C. Vreeland
William S. Blaner
Noa Noy
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  organization: Department of Medicine, College of Physicians and Surgeons, Columbia University
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  givenname: Amanda C.
  surname: Vreeland
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  organization: Nutrition, Case Western Reserve University School of Medicine
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Snippet Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
The plasma membrane protein STRA6 transports vitamin A from its blood carrier retinol binding protein (RBP) into cells, and it also functions as a cytokine...
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StartPage 3164
SubjectTerms 3T3 Cells
Animals
Biological Transport, Active
Cell Line, Tumor
Cell Physiological Phenomena
Hep G2 Cells
Humans
Male
Membrane Proteins - metabolism
Mice
Receptors, Cell Surface - metabolism
Retinol-Binding Proteins - metabolism
Signal Transduction
Vitamin A - metabolism
Title Cross Talk between Signaling and Vitamin A Transport by the Retinol-Binding Protein Receptor STRA6
URI http://mcb.asm.org/content/32/15/3164.abstract
https://www.tandfonline.com/doi/abs/10.1128/MCB.00505-12
https://www.ncbi.nlm.nih.gov/pubmed/22665496
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