Peroxisome biogenesis disorders

Steinberg, Steven J.; Dodt, Gabriele; Raymond, Gerald V.; Braverman, Nancy; Moser, Ann B.; Moser, Hugo W.

doi:10.1016/j.bbamcr.2006.09.010

Cited by 458 publications

(404 citation statements)

References 131 publications

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“…In humans, the latter results in a spectrum of genetic diseases called peroxisome biogenesis disorders, depending on the defective gene (Steinberg et al, 2006) (see Table 1). In other multicellular organisms, defects in peroxisome assembly also result in multiple biochemical and developmental abnormalities (Thieringer et al, 2003;Nito et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes

Lanyon‐Hogg

Warriner

Baker

2010

Biology of the Cell

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Peroxisomes are a family of organelles which have many unusual features. They can arise de novo from the endoplasmic reticulum by a still poorly characterized process, yet possess a unique machinery for the import of their matrix proteins. As peroxisomes lack DNA, their function, which is highly variable and dependent on developmental and/or environmental conditions, is determined by the post-translational import of specific metabolic enzymes in folded or oligomeric states. The two classes of matrix targeting signals for peroxisomal proteins [PTS1 (peroxisomal targeting signal 1) and PTS2] are recognized by cytosolic receptors [PEX5 (peroxin 5) and PEX7 respectively] which escort their cargo proteins to, or possibly across, the peroxisome membrane. Although the membrane translocation mechanism remains unclear, it appears to be driven by thermodynamically favourable binding interactions. Recycling of the receptors from the peroxisome membrane requires ATP hydrolysis for two linked processes: ubiquitination of PEX5 (and the PEX7 co-receptors in yeast) and the function of two peroxisome-associated AAA (ATPase associated with various cellular activities) ATPases, which play a role in recycling or turnover of the ubiquitinated receptors. This review summarizes and integrates recent findings on peroxisome matrix protein import from yeast, plant and mammalian model systems, and discusses some of the gaps in our understanding of this remarkable protein transport system.

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Section: Introductionmentioning

confidence: 99%

Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes

Lanyon‐Hogg

Warriner

Baker

2010

Biology of the Cell

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“…Incomplete peroxisomes fail to perform their metabolic duties including the b-oxidation of fatty acids with a chain length of more than 22 carbons, the a-oxidation of phytanic acid and similar compounds, pipecolic acid oxidation, and early plasmalogen synthesis. 6 The intracellular accumulation of VLCFA damages developing organs (e.g. liver, bone, kidneys) and is especially deleterious to the organizing brain.…”

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confidence: 99%

“…6 The proper assembly of a peroxisome requires a unique set of proteins termed "peroxins." Peroxins help incorporate enzymes into the forming peroxisome's matrix.…”

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confidence: 99%

Child Neurology: Zellweger syndrome

Lee

Raymond

2013

Neurology

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“…If the concentration of VLCFAs, phytanic and pristanic acid (depending on the diet) are elevated and concentrations of plasmalogens are decreased the diagnosis of a ZSS is established biochemically. 11 If concentrations of VLCFAs are within the normal range and biosynthesis of plasmalogens in erythrocytes is also within the normal range or is only slightly decreased, but the clinical presentation strongly points to a PBD, we recommend a skin biopsy to culture primary human fibroblasts (PHFs). Measurement of the concentration of VLCFAs, as well as biosynthesis of plasmalogens, should be repeated in these PHFs.…”

Section: Methodsmentioning

confidence: 99%