Related Experiment Video
Updated: Apr 20, 2026

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
Published on: July 20, 2022
In silico aided thoughts on mitochondrial vitamin C transport
1Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, 1111 Szent Gellért tér 4, Budapest, Hungary; Pathobiochemistry Research Group of Hungarian Academy of Sciences and Semmelweis University, 1444 Budapest, PO Box 260, Budapest, Hungary.
Abstract:
The huge demand of mitochondria as the quantitatively most important sources of ROS in the majority of heterotrophic cells for vitamin C is indisputable. The reduced form of the vitamin, l-ascorbic acid, is imported by an active mechanism requiring two sodium-dependent vitamin C transporters (SVCT1 and SVCT2). The oxidized form, dehydroascorbate is taken up by different members of the GLUT family. Because of the controversial experimental results the picture on mitochondrial vitamin C transport became quite obscure by the spring of 2014. Thus in silico prediction tools were applied in aid of the support of in vitro and in vivo results. The role of GLUT1 as a mitochondrial dehydroascorbate transporter could be reinforced by in silico predictions however the mitochondrial presence of GLUT10 is not likely since this transport protein got far the lowest mitochondrial localization scores. Furthermore the possible roles of GLUT9 and 11 in mitochondrial vitamin C transport can be proposed leastwise on the base of their computational localization analysis. In good concordance with the newest experimental observations on SVCT2 the mitochondrial presence of this transporter could also be supported by the computational prediction tools.
More Related Videos
08:37Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution
Published on: June 1, 2017
08:03Unveiling Xenobiotic Transport and Effects in Isolated Mitochondria: Insights from Respirometric and Enzymatic Assays
Published on: March 7, 2025
Related Concept Videos
Protein Transport into the Inner Mitochondrial Membrane
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Mitochondrial Protein Sorting
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
The Significance of Membrane Transport
Transporters facilitate either an active or passive movement of solutes. They can allow a single-molecule transport down its...
Energy to Drive Translocation
Generally, polypeptides are unfolded by two distinct...
Mitochondrial Precursor Proteins
Most of the mitochondrial...