Metabolite Transporters of the Plant Peroxisomal Membrane: Known and Unknown

Chapter
Part of the Subcellular Biochemistry book series (SCBI, volume 69)

Abstract

Tremendous progress in plant peroxisome research has revealed unexpected metabolic functions for plant peroxisomes. Besides photorespiration and lipid metabolism, plant peroxisomes play a key role in many metabolic and signaling pathways, such as biosynthesis of phytohormones, pathogen defense, senescence-associated processes, biosynthesis of biotin and isoprenoids, and metabolism of urate, polyamines, sulfite, phylloquinone, volatile benzenoids, and branched chain amino acids. These peroxisomal pathways require an interplay with other cellular compartments, including plastids, mitochondria, and the cytosol. Consequently, a considerable number of substrates, intermediates, end products, and cofactors have to shuttle across peroxisome membranes. However, our knowledge of their membrane passage is still quite limited. This review describes the solute transport processes required to connect peroxisomes with other cell compartments. Furthermore, we discuss the known and yet-to-be-defined transport proteins that mediate these metabolic exchanges across the peroxisomal bilayer.

Keywords

Plant Peroxisomes Metabolite transport proteins 

Abbreviations

AA

Amino acid

AAE

Acyl-activating enzyme

ABC

ATP binding cassette

ABI5

Abscisic acid-insensitive 5

APX

Ascorbate peroxidase

ASC

Ascorbate

ATP

Adenosine triphosphate

BA

Benzoic acid

BCAA

Branched chain amino acid

β-ox

β-oxidation

BZO1

Benzoyl-CoA ligase

CHY1/DBR5

Peroxisomal β-hydroxyisobutyryl-CoA hydrolase

CoA

Coenzyme A

CTS

COMATOSE (peroxisomal ABC transporter)

2,4-D

Dichlorophenoxyacetic acid

DAR

Dehydroascorbate reductase

2,4-DB

2,4-dichlorophenoxybutyrate

D-2-HG

D-2-hydroxyglutarate

DHNA

1,4-dihydroxy-2-naphthoate

DiT2

Glutamate/2-oxoglutarate translocator

DMAPP

Dimethylallyl diphosphate

DOXP

1-deoxy-D-xylulose-5-phosphate

FA

Fatty acid

FFS

Farnesyl diphosphate synthase

GAP

Glycerinaldehyde 3-phosphate

Glu

Glutamate

G6PD

Glucose-6-phosphate dehydrogenase

GR

Glutathione reductase

GSH

Glutathione

GSSH

Glutathione disulfide

H2O2

Hydrogen peroxide

IAA

Indole acetic acid (auxin)

IBA

Indole butyric acid

IDH

Isocitrate dehydrogenase

IDI

Isopentenyl diphosphate isomerase

IPP

Isopentenyl diphosphate

JA

Jasmonic acid

KAPA

7-keto-8-amino-pelargonic acid

NAD

Nicotinamide adenine dinucleotide

NADH

Nicotinamide adenine dinucleotide reduced

NADP

Nicotinamide adenine dinucleotide phosphate

NADPH

Nicotinamide adenine dinucleotide phosphate reduced

NAT

Nucleobase-ascorbate transport protein

NH4+

Ammonium

MDAR

Monodehydroascorbate reductase

MVA

Mevalonate

MVD

Mevalonate diphosphate decarboxylase

OG

2-oxoglutarate

OPC8:0

3-oxo-2-(2′-[Z]-pentenyl)cyclopentane-1-octanoic acid

OPDA

12-oxophytodienoic acid

OPPP

Oxidative pentose phosphate pathway

PA

Polyamine

PAL

Phenylalanine ammonia lyase

PHYLLO

Plastid multifunctional enzyme

6PGD

6-phosphogluconate dehydrogenase

6PGL

6-phosphogluconolactone

PMK

Phosphomevalonate kinase

PMP22

22 kDa peroxisomal membrane protein

PNC

Peroxisomal ATP transport proteins

Pi

Inorganic phosphate

PPase

Pyrophosphatase

PPi

Pyrophosphate

PT

Plastidial phosphate translocator

PTS

Peroxisomal targeting signal

PUT1

Small aliphatic amine transporter

Pxmp2

Peroxisomal membrane protein 2

PXN

Peroxisomal NAD/CoA transport protein

Ru1.5BP

Ribulose-1.5-bisphosphate

RNAi

RNA interference

ROS

Reactive oxygen species

SA

Salicylic acid

SO

Sulfite oxidase

TCA

Tricarboxylic acid cycle

YFP

Yellow fluorescent protein

XDH

Xanthine dehydrogenase

Notes

Acknowledgements

This work was supported by the DFG-grant 1781/1-1, 1781/2-1 and GRK 1525 (to Nicole Linka). The authors are grateful to Andreas P. M. Weber for helpful discussion. Many thanks to Kristin Bernhardt, Martin Schroers, Sarah K. Vigelius, Jan Wiese, and Thomas Wrobel for their commitments to elucidate the peroxisomal permeome in plants. Rothamsted Research receives grant-aided support from the BBSRC of the UK.

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Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  1. 1.Department of Plant BiochemistryHeinrich Heine University DüsseldorfDüsseldorfGermany
  2. 2.Biological Chemistry and Crop Protection DepartmentRothamsted ResearchHarpendenUK

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