2014
DOI: 10.4161/19336950.2014.956564
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Mitochondria represent another locale for the divalent metal transporter 1 (DMT1)

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Cited by 32 publications
(29 citation statements)
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References 56 publications
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“…Recently, DMT1 was found to be located in outer mitochondrial membrane and plays roles in mitochondrial iron import and other metals. 70 The fact that iron is of vital importance for mitochondrial energy metabolism in oxidative phosphorylation as electron carriers contradicts our data where low DMT1 expression associates gene enrichment of mitochondrial function. Since our study investigated oxidative phosphorylation between high and low DMT1 expression and did not compared with DMT1 expression in the normal liver, the relatively low DMT expression does not necessarily reflect a shortage of DMT1 and iron.…”
Section: Discussioncontrasting
confidence: 98%
“…Recently, DMT1 was found to be located in outer mitochondrial membrane and plays roles in mitochondrial iron import and other metals. 70 The fact that iron is of vital importance for mitochondrial energy metabolism in oxidative phosphorylation as electron carriers contradicts our data where low DMT1 expression associates gene enrichment of mitochondrial function. Since our study investigated oxidative phosphorylation between high and low DMT1 expression and did not compared with DMT1 expression in the normal liver, the relatively low DMT expression does not necessarily reflect a shortage of DMT1 and iron.…”
Section: Discussioncontrasting
confidence: 98%
“…However, direct evidence for the movement of divalent ferrous iron across the OMM via porins remains elusive. An alternate hypothesis is that a mitochondrial isoform of DMT1, which was found to localize to the OMM in HEK293 cells, imports ferrous iron into the intermembrane space [38,39]. …”
Section: Iron Trafficking To the Mitochondriamentioning
confidence: 99%
“…The simplified view of OMM permeation involving VDAC has been challenged and complicated by recent reports identifying several OMM channel proteins and transporters (reviewed in Becker and Wagner, 2018 ), suggesting that the permeability of the OMM for electrolytes and small organic molecules is much more selective than previously thought. Moreover, we have identified the proton-coupled symporter DMT1 as a functioning OMM protein ( Wolff et al, 2014a , 2018 ) (see section “A Recent, Versatile Candidate for OMM Import of Divalent Cations”).…”
Section: Transport At Omm and Imm And Properties In Relation To Metalmentioning
confidence: 99%
“…The issue for iron can also be placed in the larger context of how selectively the OMM and IMM perform as barriers – debated above in section “Transport at OMM and IMM and Properties in Relation to Metal Ion Movement.” We considered another mechanism when we detected mitochondrial DMT1 ( Wolff et al, 2014b ) closely associated with OMM markers and confirmed by subcellular fractionation. Additional support quickly followed ( Wolff et al, 2014a ), with both works reviewed subsequently ( Thévenod and Wolff, 2016 ). Later evidence showed that DMT1 was involved in import of Fe 2+ and Mn 2+ across the OMM ( Wolff et al, 2018 ).…”
Section: A Recent Versatile Candidate For Omm Import Of Divalent Catmentioning
confidence: 99%
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