title: Metabolite transport across the peroxisomal membrane.
abstract: In recent years, much progress has been made with respect to the unravelling of the functions of peroxisomes in metabolism, and it is now well established that peroxisomes are indispensable organelles, especially in higher eukaryotes. Peroxisomes catalyse a number of essential metabolic functions including fatty acid beta-oxidation, ether phospholipid biosynthesis, fatty acid alpha-oxidation and glyoxylate detoxification. The involvement of peroxisomes in these metabolic pathways necessitates the transport of metabolites in and out of peroxisomes. Recently, considerable progress has been made in the characterization of metabolite transport across the peroxisomal membrane. Peroxisomes posses several specialized transport systems to transport metabolites. This is exemplified by the identification of a specific transporter for adenine nucleotides and several half-ABC (ATP-binding cassette) transporters which may be present as hetero- and homo-dimers. The nature of the substrates handled by the different ABC transporters is less clear. In this review we will describe the current state of knowledge of the permeability properties of the peroxisomal membrane.
authors.affiliation: University of Amsterdam, Academic Medical Centre, Department of Clinical Chemistry and Pediatrics, Laboratory Genetic Metabolic Diseases, F0-224, Meibergdreef 9, Amsterdam, 1105 AZ The Netherlands. w.f.visser@amc.uva.nl
authors.forename: Wouter F
authors.initials: WF
authors.lastname: Visser
authors.forename: Carlo W T
authors.initials: CW
authors.lastname: van Roermund
authors.forename: Lodewijk
authors.initials: L
authors.lastname: Ijlst
authors.forename: Hans R
authors.initials: HR
authors.lastname: Waterham
authors.forename: Ronald J A
authors.initials: RJ
authors.lastname: Wanders
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000502:physiology*; D026921:Amino Acid Transport Systems, Neutral / Q000378:metabolism; D000818:Animals; D029681:Arabidopsis Proteins / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D005227:Fatty Acids / Q000378:metabolism*; D005230:Fatty Acids, Nonesterified / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007425:Intracellular Membranes / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D000074401:Peroxins; D020675:Peroxisomes / Q000378:metabolism*; D010944:Plants / Q000378:metabolism; D018272:Porins / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism
chemical_list: C431523:ANT1 protein, Arabidopsis; D018528:ATP-Binding Cassette Transporters; D026921:Amino Acid Transport Systems, Neutral; D029681:Arabidopsis Proteins; D002135:Calcium-Binding Proteins; D005227:Fatty Acids; D005230:Fatty Acids, Nonesterified; D008565:Membrane Proteins; D018832:Molecular Chaperones; C092128:PEX11 protein, S cerevisiae; C489785:PXMP2 protein, human; C120047:PXMP4 protein, human; D000074401:Peroxins; D018272:Porins; C101767:SSC1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C116693:peroxisomal membrane protein 34; D009243:NAD; D009249:NADP; D000252:Calcium-Transporting ATPases