Compartmentalization of the plant peroxin, AtPex10p, within subdomain(s) of ER

Flynn, Charles R.; Heinze, Michael; Schümann, Uwe; Gietl, Christine; Trelease, Richard N.

doi:10.1016/j.plantsci.2004.09.030

Cited by 26 publications

(23 citation statements)

References 69 publications

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“…These proteins were considered to be of special interest, as connections between the ER and the peroxisomes in relation to peroxisomal protein import have been reported previously (Elgersma et al, 1997;Flynn et al, 2005;Karnik and Trelease, 2005). One of the proteins detected was calreticulin.…”

Section: Identification Of Er Proteinsmentioning

confidence: 89%

“…The resolution to these questions may be tightly linked to peroxisomal biogenesis and the import of peroxisomal proteins, especially those inserted into the membrane of these organelles. An involvement of the ER in the import of proteins into peroxisomes has been proposed for PEX15 in yeast (Elgersma et al, 1997) and for PEX10 and PEX16 in Arabidopsis cell suspension cultures (Flynn et al, 2005;Karnik and Trelease, 2005), although PEX10 has also been reported to be targeted to peroxisomes without a passage through the ER (Sparkes et al, 2005). BIP has been found in the same gradient fraction as APX in pumpkin (Nito et al, 2001).…”

Section: Apparently Nonperoxisomal Proteins In Peroxisome Preparationsmentioning

confidence: 99%

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Novel Proteins, Putative Membrane Transporters, and an Integrated Metabolic Network Are Revealed by Quantitative Proteomic Analysis of Arabidopsis Cell Culture Peroxisomes

et al. 2008

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Peroxisomes play key roles in energy metabolism, cell signaling, and plant development. A better understanding of these important functions will be achieved with a more complete definition of the peroxisome proteome. The isolation of peroxisomes and their separation from mitochondria and other major membrane systems have been significant challenges in the Arabidopsis (Arabidopsis thaliana) model system. In this study, we present new data on the Arabidopsis peroxisome proteome obtained using two new technical advances that have not previously been applied to studies of plant peroxisomes. First, we followed density gradient centrifugation with free-flow electrophoresis to improve the separation of peroxisomes from mitochondria. Second, we used quantitative proteomics to identify proteins enriched in the peroxisome fractions relative to mitochondrial fractions. We provide evidence for peroxisomal localization of 89 proteins, 36 of which have not previously been identified in other analyses of Arabidopsis peroxisomes. Chimeric green fluorescent protein constructs of 35 proteins have been used to confirm their localization in peroxisomes or to identify endoplasmic reticulum contaminants. The distribution of many of these peroxisomal proteins between soluble, membrane-associated, and integral membrane locations has also been determined. This core peroxisomal proteome from nonphotosynthetic cultured cells contains a proportion of proteins that cannot be predicted to be peroxisomal due to the lack of recognizable peroxisomal targeting sequence 1 (PTS1) or PTS2 signals. Proteins identified are likely to be components in peroxisome biogenesis, b-oxidation for fatty acid degradation and hormone biosynthesis, photorespiration, and metabolite transport. A considerable number of the proteins found in peroxisomes have no known function, and potential roles of these proteins in peroxisomal metabolism are discussed. This is aided by a metabolic network analysis that reveals a tight integration of functions and highlights specific metabolite nodes that most probably represent entry and exit metabolites that could require transport across the peroxisomal membrane.Within the plant cell, energy metabolism is mainly distributed among three distinct organelles: plastids, mitochondria, and peroxisomes. Although the proteomes of both plastids and mitochondria have been investigated extensively, comparatively little systematic analysis of the protein content of plant peroxisomes has been undertaken. The main obstacle for proteomics of plant peroxisomes is the availability of purified organelles from model plants that are also amenable to mass spectrometry (MS)-based identification by matching to protein sequence data. Whereas the preparation of peroxisomes in sufficient amounts and purity from spinach (Spinacia oleracea), cucumber (Cucumis sativus), pea (Pisum sativum), and soybean (Glycine max) for proteomic purposes is possible (Schwitzguebel and Siegenthaler, 1984;Corpas et al., 1994;Lopez-Huertas et al., 1999;Arai et al., 2008), the ...

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Section: Identification Of Er Proteinsmentioning

confidence: 89%

Section: Apparently Nonperoxisomal Proteins In Peroxisome Preparationsmentioning

confidence: 99%

Novel Proteins, Putative Membrane Transporters, and an Integrated Metabolic Network Are Revealed by Quantitative Proteomic Analysis of Arabidopsis Cell Culture Peroxisomes

et al. 2008

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“…The PMPs APX3 and Arabidopsis PEX10 localize to subdomains of the rough ER (Lisenbee et al, 2003;Flynn et al, 2005;Trelease, 2005, 2007). However, whether these regions are identical and how the intra-ER sorting and segregation of APX and PEX10 (or any other PMP in the ER) is accomplished has not been elucidated.…”

Section: Membrane Protein Trafficking From the Er To Peroxisomesmentioning

confidence: 99%

“…Arabidopsis PEX10, which is reported to sort either indirectly to peroxisomes via the ER in suspension cells (Flynn et al, 2005) or directly to peroxisomes from the cytosol in leaves (Sparkes et al, 2005), also appears to perform multiple functions, including the biogenesis of ER-derived protein and oil bodies (Schumann et al, 2003), the maintenance of ER morphology, the formation of cuticular wax (Kamigaki et al, 2009), peroxisome and chloroplast connections (Schumann et al, 2007), and, as discussed further below, the import of matrix proteins (Nito et al, 2007;Prestele et al, 2010). The relative distribution of PEX10 in the ER and peroxisomes might exemplify how plant peroxisome biogenesis varies depending on the species and/or cell type.…”

Section: Membrane Protein Trafficking From the Er To Peroxisomesmentioning

confidence: 99%

Plant Peroxisomes: Biogenesis and Function

et al. 2012

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Peroxisomes are eukaryotic organelles that are highly dynamic both in morphology and metabolism. Plant peroxisomes are involved in numerous processes, including primary and secondary metabolism, development, and responses to abiotic and biotic stresses. Considerable progress has been made in the identification of factors involved in peroxisomal biogenesis, revealing mechanisms that are both shared with and diverged from non-plant systems. Furthermore, recent advances have begun to reveal an unexpectedly large plant peroxisomal proteome and have increased our understanding of metabolic pathways in peroxisomes. Coordination of the biosynthesis, import, biochemical activity, and degradation of peroxisomal proteins allows for highly dynamic responses of peroxisomal metabolism to meet the needs of a plant. Knowledge gained from plant peroxisomal research will be instrumental to fully understanding the organelle's dynamic behavior and defining peroxisomal metabolic networks, thus allowing the development of molecular strategies for rational engineering of plant metabolism, biomass production, stress tolerance, and pathogen defense.

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“…Immunolabeling of protoplasts was done as described previously (Lisenbee et al, 2003;Flynn et al, 2005) with the following modifications. Briefly, 2 to 4 d after transformation, formaldehyde-fixed protoplasts (see above) were adhered to poly-L-lysine-coated slides for 30 min, incubated in 0.33% (v/v) Triton X-100 in PBS for 15 min, and washed twice in PBS.…”

Section: Biolistic Cell Transformation and (Immuno)fluorescence Micromentioning

confidence: 99%

ArabidopsisPEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A Cooperate in Cell Cycle–Associated Replication of Peroxisomes

et al. 2008

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Although participation of PEROXIN11 (PEX11), FISSION1 (FISl), and DYNAMIN-RELATED PROTEIN (DRP) has been well established during induced peroxisome proliferation in response to external stimuli, their roles in cell cycle-associated constitutive replication/duplication have not been fully explored. Herein, bimolecular fluorescence complementation experiments with Arabidopsis thaliana suspension cells revealed homooligomerization of all five PEX11 isoforms (PEX11a-e) and heterooligomerizations of all five PEX11 isoforms with FIS1b, but not FIS1a nor DRP3A. Intracellular protein targeting experiments demonstrated that FIS1b, but not FIS1a nor DRP3A, targeted to peroxisomes only when coexpressed with PEX11d or PEX11e. Simultaneous silencing of PEX11c-e or individual silencing of DRP3A, but not FIS1a nor FIS1b, resulted in ;40% reductions in peroxisome number. During G2 in synchronized cell cultures, peroxisomes sequentially enlarged, elongated, and then doubled in number, which correlated with peaks in PEX11, FIS1, and DRP3A expression. Overall, these data support a model for the replication of preexisting peroxisomes wherein PEX11c, PEX11d, and PEX11e act cooperatively during G2 to promote peroxisome elongation and recruitment of FIS1b to the peroxisome membrane, where DRP3A stimulates fission of elongated peroxisomes into daughter peroxisomes, which are then distributed between daughter cells.

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Compartmentalization of the plant peroxin, AtPex10p, within subdomain(s) of ER

Cited by 26 publications

References 69 publications

Novel Proteins, Putative Membrane Transporters, and an Integrated Metabolic Network Are Revealed by Quantitative Proteomic Analysis of Arabidopsis Cell Culture Peroxisomes

Novel Proteins, Putative Membrane Transporters, and an Integrated Metabolic Network Are Revealed by Quantitative Proteomic Analysis of Arabidopsis Cell Culture Peroxisomes

Plant Peroxisomes: Biogenesis and Function

ArabidopsisPEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A Cooperate in Cell Cycle–Associated Replication of Peroxisomes

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