Peroxisomes and peroxisomal disorders: The main facts

Fidaleo, Marco

doi:10.1016/j.etp.2009.08.008

Cited by 39 publications

(27 citation statements)

References 120 publications

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“…A role for peroxisomes in ageing and inflammation response has also been suggested (12)(13)(14). Consequently, the absence of functional peroxisomes causes severe diseases eventually leading to early death, e.g., Zellweger spectrum diseases such as the Zellweger syndrome, neonatal adrenoleukodystrophy or infantile Refsum disease (15)(16)(17). Similarly, yeast mutant cells lacking peroxisomes are unable to grow on media containing fatty acids as the sole carbon source, but they can easily ferment if the culture medium is supplemented with sugars such as glucose (18,19).…”

Section: The Peroxisome a Dynamically Shaped Organellementioning

confidence: 99%

Membrane elongation factors in organelle maintenance: the case of peroxisome proliferation

Koch

Brocard

2011

BioMolecular Concepts

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Separation of metabolic pathways in organelles is critical for eukaryotic life. Accordingly, the number, morphology and function of organelles have to be maintained through processes linked with membrane remodeling events. Despite their acknowledged significance and intense study many questions remain about the molecular mechanisms by which organellar membranes proliferate. Here, using the example of peroxisome proliferation, we give an overview of how proteins elongate membranes. Subsequent membrane fission is achieved by dynamin-related proteins shared with mitochondria. We discuss basic criteria that membranes have to fulfill for these fission factors to complete the scission. Because peroxisome elongation is always associated with unequal distribution of matrix and membrane proteins, we propose peroxisomal division to be non-stochastic and asymmetric. We further show that these organelles need not be functional to carry on membrane elongation and present the most recent findings concerning members of the Pex11 protein family as membrane elongation factors. These factors, beside known proteins such as BAR-domain proteins, represent another family of proteins containing an amphipathic α-helix with membrane bending activity.

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Section: The Peroxisome a Dynamically Shaped Organellementioning

confidence: 99%

Membrane elongation factors in organelle maintenance: the case of peroxisome proliferation

Koch

Brocard

2011

BioMolecular Concepts

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“…Rhizomelic chondrodysplasia punctata type 1 (RCDP1) is a peroxisome biogenesis disorder involving mutations in PEX7, the peroxisome transporter required for the import of enzymes involved in the synthesis of plasmalogens [1][2][3]. Insertion of a fatty alcohol via an ether linkage at sn-1 of the glycerol backbone of glycerophospholipids only occurs in peroxisomes.…”

Section: Introductionmentioning

confidence: 99%

Lipidomics Analysis of Peroxisomal Disorders: Discovery of Deficits in Phosphatidyglycerol Levels in Rhizomelic Chondrodysplasia Type 1

Wood¹,

Braverman²

2014

J Data Mining Genomics Proteomics

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Objectives: Decreases in the levels of plasmalogens, have been consistently demonstrated in rhizomelic chondrodysplasia type 1 (RCDP1), a genetic disorder of peroxisomal function. However, an in-depth lipidomics analysis has not been undertaken. We undertook such an analysis. Study Design:We performed a high-resolution mass spectrometric shotgun lipidomics analyses of plasma and lymphoblasts from RCDP1 patients. Results:We report for the first time, decrements in phosphatidylglycerol levels in plasma and lymphoblasts from RCDP1 patients. Phosphatidylinositol and phosphatidylserine levels also were unaltered in plasma and lymphoblasts. These data suggested that decrements in phosphatidylglycerol were due to increased catabolism, possibly in failed cellular attempts to restore deficient plasmalogen levels. This conclusion was further supported by supplementation of RCDP1 lymphoblasts with ether lipid plasmalogen precursors that bypass dysfunctional peroxisomes. These precursors augmented cellular levels of plasmalogens in control and RCDP1 lymphoblasts but only augmented phosphatidylglycerols in RCDP1 lymphoblasts. Conclusions:Overall, our results indicate that the peroxisomal disorder, RCDP1, which is characterized by plasmalogen deficits, also possess decrements in phosphatidylglycerol levels, thereby also compromising mitochondrial function and pulmonary surfactant synthesis. Given the role pf phosphatidylglycerols in surfactant, these new data potentially explain the severe respiratory compromise in RCDP children and may add a new parameter of mitochondrial dysfunction in these patients.

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“…Several inborn human disorders are caused by peroxisome dysfunction. Patients with these disorders, collectively called the peroxisome biogenesis disorders, exhibit a variety of physiological abnormalities due to the absence of functional peroxisomes, and usually die within their first year (Fidaleo, 2010;Steinberg et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…Peroxisomes are ubiquitous membrane-bounded organelles involved in a variety of important biochemical and metabolic processes, notably the b-oxidation of fatty acids and the detoxification of reactive oxygen species (Fidaleo, 2010;Islinger et al, 2010). Peroxisomes also function as platforms for complex cellular signaling pathways such as those acting in antiviral innate immunity (Berg et al, 2012;Dixit et al, 2010;Horner et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Dynein light chain interaction with the peroxisomal import docking complex modulates peroxisome biogenesis in yeast

Chang

Tower

Lancaster

et al. 2013

Journal of Cell Science

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SummaryDynein is a large macromolecular motor complex that moves cargo along microtubules. A motor-independent role for the light chain of dynein, Dyn2p, in peroxisome biology in Saccharomyces cerevisiae was suggested from its interaction with Pex14p, a component of the peroxisomal matrix protein import docking complex. Here we show that cells of the yeast Yarrowia lipolytica deleted for the gene encoding the homologue of Dyn2p are impaired in peroxisome function and biogenesis. These cells exhibit compromised growth on medium containing oleic acid as the carbon source, the metabolism of which requires functional peroxisomes. Their peroxisomes have abnormal morphology, atypical matrix protein localization, and an absence of proteolytic processing of the matrix enzyme thiolase, which normally occurs upon its import into the peroxisome. We also show physical and genetic interactions between Dyn2p and members of the docking complex, particularly Pex17p. Together, our results demonstrate a role for Dyn2p in the assembly of functional peroxisomes and provide evidence that Dyn2p acts in cooperation with the peroxisomal matrix protein import docking complex to effect optimal matrix protein import.

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Peroxisomes and peroxisomal disorders: The main facts

Cited by 39 publications

References 120 publications

Membrane elongation factors in organelle maintenance: the case of peroxisome proliferation

Membrane elongation factors in organelle maintenance: the case of peroxisome proliferation

Lipidomics Analysis of Peroxisomal Disorders: Discovery of Deficits in Phosphatidyglycerol Levels in Rhizomelic Chondrodysplasia Type 1

Dynein light chain interaction with the peroxisomal import docking complex modulates peroxisome biogenesis in yeast

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