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Comment
. 2012 Dec;122(12):4328-30.
doi: 10.1172/JCI66607. Epub 2012 Nov 26.

Mitochondrial heme: an exit strategy at last

Mark D Fleming  1 , Iqbal Hamza
Affiliations
Comment

Mitochondrial heme: an exit strategy at last

Mark D Fleming et al. J Clin Invest. 2012 Dec.

Abstract

The transport of heme across membranes is critical for iron absorption, the formation of hemoglobin and other hemoproteins, and iron recycling in macrophages. However, the identity of heme transport proteins has been elusive. In this issue of the JCI, Chiabrando et al. reveal that an isoform of the feline leukemia virus subgroup C receptor (FLVCR1) exports heme from the mitochondria and is critical for erythroid differentiation.

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Figures

Figure 1
Figure 1. Two isoforms of FLVCR1 may regulate heme levels.
FLVCRa isoform had previously been postulated to transport cytosolic heme across the plasma membrane. Chiabrando et al. now show that a mitochondrial isoform, FLVCR1b, transports heme from the mitochondria into the cytosol and thus is critical for the synthesis of hemoglobin and differentiation of erythroid cells.
See this image and copyright information in PMC

Comment on

  • The mitochondrial heme exporter FLVCR1b mediates erythroid differentiation.
    Chiabrando D, Marro S, Mercurio S, Giorgi C, Petrillo S, Vinchi F, Fiorito V, Fagoonee S, Camporeale A, Turco E, Merlo GR, Silengo L, Altruda F, Pinton P, Tolosano E. Chiabrando D, et al. J Clin Invest. 2012 Dec;122(12):4569-79. doi: 10.1172/JCI62422. Epub 2012 Nov 26. J Clin Invest. 2012. PMID: 23187127 Free PMC article.

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