<i>Caenorhabditis elegans</i> has a single pathway to target matrix proteins to peroxisomes

Motley, Alison M.; Hettema, Ewald H.; Ketting, René F.; Plasterk, Ronald H.A.; Tabak, Henk F.

doi:10.1093/embo-reports/kvd010

Cited by 107 publications

(89 citation statements)

References 31 publications

(64 reference statements)

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“…Note that since this heat-shock promoter is not active in all cell types, our results do not exclude the existence of peroxisomes in other tissues such as neuronal cells. Our results and the results of other groups with targeting GFP to the peroxisome prove that C. elegans contains functional peroxisomal import machinery that is dependent on SKL (Motley et al, 2000;Taub et al, 1999). These results extend characterization of the remarkable conservation of peroxisome biogenesis to include the nematode C. elegans.…”

Section: Visualization Of Peroxisomes In C Eleganssupporting

confidence: 79%

Modeling human peroxisome biogenesis disorders in the nematodeCaenorhabditis elegans

Thieringer

Moellers

Dodt

et al. 2003

Journal of Cell Science

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Peroxisomes are ubiquitous eukaryotic organelles. The proteins required for peroxisome biogenesis are called peroxins, and mutations in the peroxin genes cause the devastating human developmental syndromes called the peroxisome biogenesis disorders. Our interest is in elaborating the roles that peroxisomes play in Caenorhabditis elegans development, and in establishing an invertebrate model system for the human peroxisome biogenesis disorders. The genome of C. elegans encodes homologs of 11 of the 13 human peroxins. We disrupted five nematode peroxins using RNA interference(RNAi) and found that RNAi knockdown of each one causes an early larval arrest at the L1 stage. Using a green fluorescent protein reporter targeted to the peroxisome, we establish that peroxisomal import is impaired in prx-5(RNAi) nematodes. prx-5(RNAi) animals are blocked very early in the L1 stage and do not initiate normal postembryonic cell divisions,similar to starvation-arrested larvae. Cell and axonal migrations that normally occur during the L1 stage also appear blocked. We conclude that peroxisome function is required for C. elegans postembryonic development and that disruption of peroxisome assembly by prx-5(RNAi)prevents scheduled postembryonic cell divisions. Defects in the cellular localization of peroxisomal proteins and in development are shared features of human and nematode peroxisome biogenesis disorders. In setting up a C. elegans model of peroxisomal biogenesis disorders, we suggest that genetic screens for suppression of the Prx developmental block will facilitate identification of novel intervention strategies and may provide new insights into human disease pathogenesis.

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Section: Visualization Of Peroxisomes In C Eleganssupporting

confidence: 79%

Modeling human peroxisome biogenesis disorders in the nematodeCaenorhabditis elegans

Thieringer

Moellers

Dodt

et al. 2003

Journal of Cell Science

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“…The number of PTS2-targeted proteins ranges from zero in Caenorhabditis elegans, which has lost the PTS2 import pathway altogether (Motley et al, 2000), to an estimated 60 in A. thaliana (Reumann et al, 2009). Interestingly, S. cerevisiae appears to maintain a PTS2 import pathway solely for the transport of 3-ketoacyl thiolase (Grunau et al, 2009).…”

Section: Pts2 Pathwaymentioning

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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“…3; Helm et al, 2007;Schuhmann et al, 2008). Although plants, yeast, and mammals use both PTS1 and PTS2 systems, nematodes and fruit flies lack PTS2 proteins (Gurvitz et al, 2000;Motley et al, 2000;Faust et al, 2012).…”

Section: Matrix Protein Import: Cycling Receptorsmentioning

confidence: 99%

Peroxisome Function, Biogenesis, and Dynamics in Plants

2017

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Caenorhabditis elegans has a single pathway to target matrix proteins to peroxisomes

Cited by 107 publications

References 31 publications

Modeling human peroxisome biogenesis disorders in the nematodeCaenorhabditis elegans

Modeling human peroxisome biogenesis disorders in the nematodeCaenorhabditis elegans

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

Peroxisome Function, Biogenesis, and Dynamics in Plants

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