Peroxisomal Transport Systems: Roles in Signaling and Metabolism

Theodoulou, F. L.; Zhang, Xuebin; Lousa, Carine De Marcos; Nyathi, Yvonne; Baker, Alison

doi:10.1007/978-3-642-14369-4_12

Cited by 3 publications

(10 citation statements)

References 132 publications

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“…Although production of indole acetic acid (IAA) from IBA was not initially considered to be a major biosynthetic route, β-oxidation has since been shown to provide a significant source of IAA in seedlings, playing roles in lateral root development, expansion of root hairs and cotyledons and also contributing to stamen filament elongation in flowers (Zolman et al 2001;Footitt et al 2007;Strader et al 2010Strader et al , 2011Theodoulou et al 2011). …”

Section: β-Oxidation Of Auxinsmentioning

confidence: 99%

“…Since plants do not synthesise or use cobalamin (Croft et al 2005), it seems likely that AtABCD2 and its plant homologues carry out a different function, which has yet to be determined but is likely to be associated with photosynthesis. Dietrich et al (2009) Our current knowledge of plant peroxisomal ABC transporter function has largely been obtained from characterisation of Arabidopsis mutants, in part because CTS (AtABCD1) was identified in at least five independent forward genetic screens, each affording different insights into its biochemical and physiological functions (reviewed in Theodoulou et al 2011). Taken together, the available evidence strongly supports a model in which CTS is a broad specificity transporter which serves to import the diverse range of substrates which are processed by β-oxidation in plants.…”

Section: The Abcd Subfamily In Plantsmentioning

confidence: 99%

“…A handful of specific transporters has been discovered but it is not yet clear to what extent these account for the many transport steps which are required for to peroxisomes to fulfil their diverse functions (reviewed in Theodoulou et al 2011;Antonenkov and Hiltunen 2012;Linka and Theodoulou 2013). Amongst the best studied peroxisomal transporters are the ATP-Binding Cassette (ABC) transporters which mediate import of substrates for β-oxidation.…”

Section: Introduction and Historical Backgroundmentioning

confidence: 99%

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Plant Peroxisomal ABC Transporters: Flexible and Unusual

Theodoulou

Baldwin

et al. 2014

Signaling and Communication in Plants

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ABC transporters of subfamily D mediate import of substrates for β-oxidation into peroxisomes. Whilst mammals possess three peroxisomal ABCD proteins which homodimerise to form transporters with distinct substrate specificities, Baker's yeast has a single transporter formed by heterodimerisation, which imports long-chain fatty acyl CoAs. Plants have a single-fused heterodimer transporter that exhibits broad substrate specificity, reflecting the wide range of β-oxidation substrates processed by plants. The fusion appears to have occurred early in the evolution of land plants and was followed by an early duplication event in the monocot lineage. Plant ABCD proteins function in all stages of the life cycle and their physiological roles reflect the ability to transport diverse substrates including saturated and unsaturated fatty acids and aromatic compounds such as precursors of hormones and secondary metabolites. Recent work suggests that transport of CoA substrates involves their cleavage and re-esterification within the peroxisome, thus interaction with appropriate acyl adenylate-activating enzymes potentially provides a mechanism for regulating entry of different substrates into β-oxidation. The mechanism of ABCD transporter targeting is broadly conserved across kingdoms but evidence suggests the regulation of protein turnover differs.

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Section: β-Oxidation Of Auxinsmentioning

confidence: 99%

Section: The Abcd Subfamily In Plantsmentioning

confidence: 99%

Section: Introduction and Historical Backgroundmentioning

confidence: 99%

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Plant Peroxisomal ABC Transporters: Flexible and Unusual

Theodoulou

Baldwin

et al. 2014

Signaling and Communication in Plants

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“…Several independent forward genetic screens identified the peroxisomal ABC transporter in Arabidopsis , here referred to as COMATOSE (CTS, At4g39850; Theodoulou et al, 2006, 2011). Pro- and eukaryotic ABC transporters (TC 3.A.1), in general, are composed of two transmembrane domains and two ABC.…”

Section: The Peroxisomal Abc Transportermentioning

confidence: 99%

“…Both pathways, the breakdown of fatty acids and the photorespiratory C 2 cycle, necessitate an efficient flux of metabolites and cofactors between peroxisomes and other cellular compartments. These transport processes across the single bilayer are important, because they connect and control the peroxisomal metabolism with that of the other organelles (Theodoulou et al, 2011 ). A “two-channel” concept describes the permeability of the peroxisome membrane that consists of channel-forming proteins or “porins” along with specific transport proteins (Antonenkov and Hiltunen, 2006 ; Visser et al, 2007 ).…”

Section: Introductionmentioning

confidence: 99%

Transport Proteins Regulate the Flux of Metabolites and Cofactors Across the Membrane of Plant Peroxisomes

Linka

Eßer

2012

Front. Plant Sci.

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In land plants, peroxisomes play key roles in various metabolic pathways, including the most prominent examples, that is lipid mobilization and photorespiration. Given the large number of substrates that are exchanged across the peroxisomal membrane, a wide spectrum of metabolite and cofactor transporters is required and needs to be efficiently coordinated. These peroxisomal transport proteins are a prerequisite for metabolic reactions inside plant peroxisomes. The entire peroxisomal “permeome” is closely linked to the adaption of photosynthetic organisms during land plant evolution to fulfill and optimize their new metabolic demands in cells, tissues, and organs. This review assesses for the first time the distribution of these peroxisomal transporters within the algal and plant species underlining their evolutionary relevance. Despite the importance of peroxisomal transporters, the majority of these proteins, however, are still unknown at the molecular level in plants as well as in other eukaryotic organisms. Four transport proteins have been recently identified and functionally characterized in Arabidopsis so far: one transporter for the import of fatty acids and three carrier proteins for the uptake of the cofactors ATP and NAD into plant peroxisomes. The transport of the three substrates across the peroxisomal membrane is essential for the degradation of fatty acids and fatty acids-related compounds via β-oxidation. This metabolic pathway plays multiple functions for growth and development in plants that have been crucial in land plant evolution. In this review, we describe the current state of their physiological roles in Arabidopsis and discuss novel features in their putative transport mechanisms.

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The Saccharomyces cerevisiae ABC subfamily D transporter Pxa1/Pxa2p co‐imports CoASH into the peroxisome

et al. 2020

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ATP‐binding cassette (ABC) subfamily D transporters are important for the uptake of fatty acids and other beta‐oxidation substrates into peroxisomes. Genetic and biochemical evidence indicates that the transporters accept fatty acyl‐coenzyme A that is cleaved during the transport cycle and then re‐esterified in the peroxisomal lumen. However, it is not known whether free coenzyme A (CoA) is released inside or outside the peroxisome. Here we have used Saccharomyces cerevisiae and isolated peroxisomes to demonstrate that free CoA is released in the peroxisomal lumen. Thus, ABC subfamily D transporter provide an import pathway for free CoA that controls peroxisomal CoA homeostasis and tunes metabolism according to the cell’s demands.

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Peroxisomal Transport Systems: Roles in Signaling and Metabolism

Cited by 3 publications

References 132 publications

Plant Peroxisomal ABC Transporters: Flexible and Unusual

Plant Peroxisomal ABC Transporters: Flexible and Unusual

Transport Proteins Regulate the Flux of Metabolites and Cofactors Across the Membrane of Plant Peroxisomes

The Saccharomyces cerevisiae ABC subfamily D transporter Pxa1/Pxa2p co‐imports CoASH into the peroxisome

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