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Cited by 100Retinoids in leukemia and cellular processesCytokine Signaling Pathways and InteractionsAdipokines, Inflammation, and Metabolic Diseases

Signaling by vitamin A and retinol-binding protein in regulation of insulin responses and lipid homeostasis

Open access
Berry, Daniel C., Noy, Noa·2012·Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
DOI 10.1016/j.bbalip.2011.07.002PMC PMC3204314
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Abstract

Vitamin A, retinol, circulates in blood bound to serum retinol binding protein (RBP) and is transported into cells by a membrane protein termed stimulated by retinoic acid 6 (STRA6). It was reported that serum levels of RBP are elevated in obese rodents and humans, and that increased level of RBP in blood causes insulin resistance. A molecular mechanism by which RBP can exert such an effect is suggested by the recent discovery that STRA6 is not only a vitamin A transporter but also functions as a surface signaling receptor. Binding of RBP-ROH to STRA6 induces the phosphorylation of a tyrosine residue in the receptor C-terminus, thereby activating a JAK/STAT signaling cascade. Consequently, in STRA6-expressing cells such as adipocytes, RBP-ROH induces the expression of STAT target genes, including SOCS3, which suppresses insulin signaling, and PPARγ, which enhances lipid accumulation. RBP-retinol thus joins the myriad of cytokines, growth factors and hormones which regulate gene transcription by activating cell surface receptors that signal through activation of Janus kinases and their associated transcription factors STATs. This article is part of a Special Issue entitled Retinoid and Lipid Metabolism.

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Crossref · 10.1016/j.bbalip.2011.07.002

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  • Vitamin A/retinol activates the Janus kinase/STAT5 signaling pathway.

    “Finally, vitamin A/retinol proved recently to be active and to activate the Janus kinase/STAT5 signaling pathway.”

    From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [127]

    Section 5 reports that retinol-bound RBP activates the STRA6/JAK2/STAT5 pathway. It also states that retinol alone did not trigger JAK/STAT signaling, so the claim omits an essential condition. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • RA- and retinol-induced kinases have been reported to cross talk with the transcriptional activity of RARs and other transcription factors.

    “In line with this concept, the RA-and retinol-induced kinases have been reported to cross talk with the transcriptional activity of RARs and other transcription factors.”

    From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [127]

    The Introduction and section 5 describe retinol-bound RBP activating a JAK2/STAT pathway that regulates STAT target genes. They do not report RA-induced kinase signaling or crosstalk with RAR transcriptional activity; section 5 instead describes this pathway as independent of retinoic acid and its nuclear receptors. No page number is available in our copy. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

  • This nuclear integration involves mainly phosphorylation processes that influence their DNA recruitment and the timing of the sequential recruitment of the different classes of coregulators, as well as the stability of the phosphorylated proteins.

    “This nuclear integration involves mainly phosphorylation processes that infl uence their DNA recruitment and the timing of the sequential recruitment of the different classes of coregulators, as well as the stability of the phosphorylated proteins.”

    From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [127]

    Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.

    Experimental — accuracy not yet measured

  • Retinol associated to RBP and bound to the cell surface signaling receptor Stra6 was found to activate the JAK/STAT5 signaling cascade.

    “Indeed retinol that was associated to the “retinol-binding protein (RBP)” and that was bound to the cell surface signaling receptor stimulated by retinoic acid 6 (Stra6) was found to activate the Janus kinases (JAK)/signal transducer and activator of transcription 5 (STAT5) signaling cascade ( 126-128 ) ( Fig. 5B ).”

    From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [127]

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Authors
Berry, D. C., & Noy, N.
Affiliations
Case Western Reserve University (US)
Corresponding author
Noy, Noa
ORCID
Venue
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
Publisher
Elsevier BV
Published
2012-01
Volume
1821
Issue
1
Pages
168-176
ISSN
1388-1981 (ISSN-L)
DOI
10.1016/j.bbalip.2011.07.002
PMC
PMC3204314
OpenAlex
W1975618241
Cited by
100
References
88
Citations by year
2026: 2 · 2025: 3 · 2024: 3 · 2023: 3 · 2022: 1 · 2021: 10 · 2020: 2 · 2019: 3 · 2018: 2 · 2017: 10 · 2016: 10 · 2015: 18 · 2014: 9 · 2013: 9 · 2012: 15
FWCI
0.96
Type
journal article
Language
en
Open access
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
NIH (DK060684, DK088669, DK073195T32)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
  • Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
  • Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
Keywords
vitamin A, retinol-binding protein, STRA6, insulin resistance, lipid homeostasis, JAK/STAT signaling, SOCS3, PPARγ, adipocytes, obesity, retinol, cell surface receptor signaling, STAT phosphorylation
MeSH terms
Suppressor of Cytokine Signaling 3 Protein, Animals, Homeostasis, Humans, Insulin, Insulin Resistance, Lipids, Membrane Proteins, Retinol-Binding Proteins, Vitamin A, Signal Transduction, PPAR gamma, Lipid Metabolism, STAT Transcription Factors, Suppressor of Cytokine Signaling Proteins, Janus Kinases

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