Abstract
Peroxisomes are eukaryotic organelles that are essential for growth and development. They are highly metabolically active and house many biochemical reactions, including lipid metabolism and synthesis of signaling molecules. Most of these metabolic pathways are shared with other compartments, such as Endoplasmic reticulum (ER), mitochondria, and plastids. Peroxisomes, in common with all other cellular organelles are dependent on a wide range of cofactors, such as adenosine 5′-triphosphate (ATP), Coenzyme A (CoA), and nicotinamide adenine dinucleotide (NAD). The availability of the peroxisomal cofactor pool controls peroxisome function. The levels of these cofactors available for peroxisomal metabolism is determined by the balance between synthesis, import, export, binding, and degradation. Since the final steps of cofactor synthesis are thought to be located in the cytosol, cofactors must be imported into peroxisomes. This review gives an overview about our current knowledge of the permeability of the peroxisomal membrane with the focus on ATP, CoA, and NAD. Several members of the mitochondrial carrier family are located in peroxisomes, catalyzing the transfer of these organic cofactors across the peroxisomal membrane. Most of the functions of these peroxisomal cofactor transporters are known from studies in yeast, humans, and plants. Parallels and differences between the transporters in the different organisms are discussed here.
Highlights
Peroxisomes are eukaryotic organelles that are surrounded by a single lipid bilayer membrane [1,2]
In vitro uptake experiments demonstrated that both Slc25a17 proteins function redundantly with a preference towards Coenzyme A (CoA), instead of nicotinamide adenine dinucleotide (NAD) and adenosine -triphosphate (ATP), similar to the human carrier [66]. These findings suggest that Slc25a17 and Slc25a17-like functions additively as CoA transporters, which are involved in peroxisomal lipid metabolism and are essential for normal embryonic growth in zebrafish [66]
The mitochondrial carrier family (MCF) is a large family of proteins present in all eukaryotic lineages, which are present in several other cellular compartments, including peroxisomes
Summary
Peroxisomes are eukaryotic organelles that are surrounded by a single lipid bilayer membrane [1,2]. The name of this family suggests that they are exclusively located to mitochondria, several members are present in other organelles, such as peroxisomes, endoplasmic reticulum, chloroplasts, and plasma membrane [23,24,26,27,29] Despite their conserved basic structure composed of three repetitive modules, MCF proteins are highly diverse in terms of substrate specificity and transport mode. MCF members mediate a strict counter-exchange and operate as a uniporter or symporter [26,27,29,30] These features suggest that this protein family was most likely exploited as a valuable basis for a fast establishment of a subset of carriers with a broad range of different transport functions in the cell during eukaryotic evolution. This review deals with MCF proteins that are known to be peroxisomal cofactor carriers in budding yeast Saccharomyces cerevisiae, humans, and the model plant Arabidopsis thaliana and highlights the recent progress on their biochemical and physiological function for the peroxisomal metabolism
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