Genetic Interactions between PEROXIN12 and Other Peroxisome-Associated Ubiquitination Components

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dc.citation.firstpage1643en_US
dc.citation.journalTitlePlant Physiologyen_US
dc.citation.lastpage1656en_US
dc.citation.volumeNumber172en_US
dc.contributor.authorKao, Yun-Tingen_US
dc.contributor.authorFleming, Wendell A.en_US
dc.contributor.authorVentura, Meredith J.en_US
dc.contributor.authorBartel, Bonnieen_US
dc.contributor.orgBiochemistry and Cell Biology Programen_US
dc.date.accessioned2016-12-16T17:50:26Zen_US
dc.date.available2016-12-16T17:50:26Zen_US
dc.date.issued2016en_US
dc.description.abstractMost eukaryotic cells require peroxisomes, organelles housing fatty acid β-oxidation and other critical metabolic reactions. Peroxisomal matrix proteins carry peroxisome-targeting signals that are recognized by one of two receptors, PEX5 or PEX7, in the cytosol. After delivering the matrix proteins to the organelle, these receptors are removed from the peroxisomal membrane or matrix. Receptor retrotranslocation not only facilitates further rounds of matrix protein import but also prevents deleterious PEX5 retention in the membrane. Three peroxisome-associated ubiquitin-protein ligases in the Really Interesting New Gene (RING) family, PEX2, PEX10, and PEX12, facilitate PEX5 retrotranslocation. However, the detailed mechanism of receptor retrotranslocation remains unclear in plants. We identified an Arabidopsis (Arabidopsis thaliana) pex12 Glu-to-Lys missense allele that conferred severe peroxisomal defects, including impaired β-oxidation, inefficient matrix protein import, and decreased growth. We compared this pex12-1 mutant to other peroxisome-associated ubiquitination-related mutants and found that RING peroxin mutants displayed elevated PEX5 and PEX7 levels, supporting the involvement of RING peroxins in receptor ubiquitination in Arabidopsis. Also, we observed that disruption of any Arabidopsis RING peroxin led to decreased PEX10 levels, as seen in yeast and mammals. Peroxisomal defects were exacerbated in RING peroxin double mutants, suggesting distinct roles of individual RING peroxins. Finally, reducing function of the peroxisome-associated ubiquitin-conjugating enzyme PEX4 restored PEX10 levels and partially ameliorated the other molecular and physiological defects of the pex12-1 mutant. Future biochemical analyses will be needed to determine whether destabilization of the RING peroxin complex observed in pex12-1 stems from PEX4-dependent ubiquitination on the pex12-1 ectopic Lys residue.en_US
dc.identifier.citationKao, Yun-Ting, Fleming, Wendell A., Ventura, Meredith J., et al.. "Genetic Interactions between PEROXIN12 and Other Peroxisome-Associated Ubiquitination Components." <i>Plant Physiology,</i> 172, (2016) American Society of Plant Biologists: 1643-1656. http://dx.doi.org/10.1104/pp.16.01211.en_US
dc.identifier.doihttp://dx.doi.org/10.1104/pp.16.01211en_US
dc.identifier.urihttps://hdl.handle.net/1911/93728en_US
dc.language.isoengen_US
dc.publisherAmerican Society of Plant Biologistsen_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.titleGenetic Interactions between PEROXIN12 and Other Peroxisome-Associated Ubiquitination Componentsen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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