Peroxisomes, glyoxysomes and glycosomes (Review)

Michels, Paul A.M.; Moyersoen, Juliette; Krazy, Hanane; Galland, Nathalie; Herman, Murielle; Hannaert, Véronique

doi:10.1080/09687860400024186

Cited by 59 publications

(47 citation statements)

References 61 publications

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“…The paracrystalline structures observed in the cells of this tissue are difficult to positively identify without immunocytochemistry, but could be peroxisomes or glyoxysomes, organelles that play a role in breakdown of very long chain fatty acids through betaoxidation (Michels et al, 2005). Van Caeseele et al (1982) saw similar structures in B. campestris, calling them 'tubular paracrystalline structures', but did not attribute any particular function to them.…”

Section: Palisade Layermentioning

confidence: 98%

The unusual tegumental tissues of the Lunaria annua (Brassicaceae) seed: A developmental study using light and electron microscopy

Mosti

Friedman

Piccolin

et al. 2012

Flora - Morphology, Distribution, Functional Ecology of Plants

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Please cite this article in press as: Mosti, S., et al., The unusual tegumental tissues of the Lunaria annua (Brassicaceae) seed: A developmental study using light and electron microscopy. Flora (2012) With light, fluorescence, transmission electron, and environmental scanning electron microscopy we studied the development of the Lunaria annua L. (Brassicaceae) seeds in order to reveal basic anatomical information about the unusual tissues of these seeds. In particular the seed tegument tissues possess complex morphological aspects that are relevant to the biology and ecology of this plant. A sclerenchymatic tissue as the innermost layer of the teguments apparently offers robust protection for the embryo, yet is organized to be flexible. This tissue likely controls the passage of water from the tegumental layers towards the embryo. We report here the presence of tannins in the pre-sclerenchymatic layer of the unripe seed. The inner tegument also houses a spongy tissue with wide intercellular spaces. This tissue could impart buoyancy to the seeds, which possibly might be required for water transport. The structural features could indicate that Lunaria may have evolved in a Mediterranean environment, which is characterized by a long dry season, but with a large amount of rainfall concentrated in short periods. Probably, not only the typical enlarged and flattened fruits of Lunaria can easily float and be dispersed away from the mother plant, but also the seeds have this dispersal peculiarity after release from the silicules.

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Section: Palisade Layermentioning

confidence: 98%

The unusual tegumental tissues of the Lunaria annua (Brassicaceae) seed: A developmental study using light and electron microscopy

Mosti

Friedman

Piccolin

et al. 2012

Flora - Morphology, Distribution, Functional Ecology of Plants

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“…In plants, peroxisomes are essential to many metabolic processes such as lipid mobilization, the glyoxylate cycle, photorespiration, detoxification, biosynthesis, and metabolism of plant hormones (2,3). Some of these metabolic processes are coordinated by peroxisomes and other organelles, e.g., mitochondria and chloroplasts for photorespiration, lipid bodies and mitochondria for lipid mobilization, and chloroplasts for jasmonic acid biosynthesis (3)(4)(5)(6).…”

mentioning

confidence: 99%

E3 ubiquitin ligase SP1 regulates peroxisome biogenesis in Arabidopsis

Pan

Satkovich

2016

Proc. Natl. Acad. Sci. U.S.A.

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Peroxisomes are ubiquitous eukaryotic organelles that play pivotal roles in a suite of metabolic processes and often act coordinately with other organelles, such as chloroplasts and mitochondria. Peroxisomes import proteins to the peroxisome matrix by peroxins (PEX proteins), but how the function of the PEX proteins is regulated is poorly understood. In this study, we identified the Arabidopsis RING (really interesting new gene) type E3 ubiquitin ligase SP1 [suppressor of plastid protein import locus 1 (ppi1) 1] as a peroxisome membrane protein with a regulatory role in peroxisome protein import. SP1 interacts physically with the two components of the peroxisome protein docking complex PEX13-PEX14 and the (RING)-finger peroxin PEX2. Loss of SP1 function suppresses defects of the pex14-2 and pex13-1 mutants, and SP1 is involved in the degradation of PEX13 and possibly PEX14 and all three RING peroxins. An in vivo ubiquitination assay showed that SP1 has the ability to promote PEX13 ubiquitination. Our study has revealed that, in addition to its previously reported function in chloroplast biogenesis, SP1 plays a role in peroxisome biogenesis. The same E3 ubiquitin ligase promotes the destabilization of components of two distinct protein-import machineries, indicating that degradation of organelle biogenesis factors by the ubiquitin-proteasome system may constitute an important regulatory mechanism in coordinating the biogenesis of metabolically linked organelles in eukaryotes.peroxisome biogenesis | E3 ubiquitin ligase | protein import | peroxin | SP1

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“…Mutations in the corresponding genes result in the retention of peroxisomal matrix proteins in the cytosol (reviewed in Refs. [2][3][4][5]. Interestingly, these cells still contain peroxisomal membrane remnants (the so-called peroxisomal "ghosts") (6) harboring much of the protein repertoire normally found in this membrane system.…”

mentioning

confidence: 99%

“…Pex19p is an acidic largely disordered protein displaying a dual subcellular localization (cytosolic and peroxisomal) with the ability to interact with most peroxisomal membrane proteins (PMPs) 4 both in vitro and in vivo (13)(14)(15). The Pex19p domain involved in these interactions resides in the C-terminal twothirds of the peroxin (16 -18).…”

mentioning

confidence: 99%

The Import Competence of a Peroxisomal Membrane Protein Is Determined by Pex19p before the Docking Step

Pinto

Grou

Alencastre

et al. 2006

Journal of Biological Chemistry

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Biogenesis of the mammalian peroxisomal membrane requires the action of Pex3p and Pex16p, two proteins present in the organelle membrane, and Pex19p, a protein that displays a dual subcellular distribution (peroxisomal and cytosolic). Pex19p interacts with most peroxisomal intrinsic membrane proteins, but whether this property reflects its role as an import receptor for this class of proteins or a chaperone-like function in the assembly/disassembly of peroxisomal membrane proteins has been the subject of much controversy. Here, we describe an in vitro system particularly suited to address this issue. It is shown that insertion of a reporter protein into the peroxisomal membrane is a Pex3p-dependent process that does not require ATP/GTP hydrolysis. The system can be programmed with recombinant versions of Pex19p, allowing us to demonstrate that Pex19p-cargo protein complexes formed in the absence of peroxisomes are the substrates for the peroxisomal docking/ insertion machinery. Data suggesting that cargo-loaded Pex19p displays a much higher affinity for Pex3p than Pex19p alone are also provided. These results suggest that soluble Pex19p participates in the targeting of newly synthesized peroxisomal membrane proteins to the organelle membrane and support the existence of a cargo-induced peroxisomal targeting mechanism for Pex19p.

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Peroxisomes, glyoxysomes and glycosomes (Review)

Cited by 59 publications

References 61 publications

The unusual tegumental tissues of the Lunaria annua (Brassicaceae) seed: A developmental study using light and electron microscopy

The unusual tegumental tissues of the Lunaria annua (Brassicaceae) seed: A developmental study using light and electron microscopy

E3 ubiquitin ligase SP1 regulates peroxisome biogenesis in Arabidopsis

The Import Competence of a Peroxisomal Membrane Protein Is Determined by Pex19p before the Docking Step

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