Biogenesis of peroxisomes and mitochondria: linked by division

Delille, Hannah K.; Alves, Renato M. P.; Schrader, Michael

doi:10.1007/s00418-009-0561-9

Cited by 63 publications

(51 citation statements)

References 52 publications

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“…However, FIS1A and FIS1B do not seem to heterodimerize on the peroxisome in our BiFC system (see Supplemental Figure 4C online). These data collectively are in line with the current knowledge about the interplay between these proteins in mammalian cells, where the DRP proteins homooligomerize, FIS1 helps to recruit DRP proteins, and DRP, FIS1, and PEX11 may form a ternary complex (Thoms and Erdmann, 2005;Yan et al, 2005;Delille et al, 2009). It remains to be determined whether DRP3A, DRP3B, and DRP5B assemble together into polymers and mediate peroxisome division in a concerted manner, whether FIS1 homooligomerization is required for its proper function, and whether PEX11, a protein primarily responsible for peroxisome elongation, is also directly involved in the FIS1-dependent recruitment of DRPs to peroxisomes.…”

Section: Coordination Between the Fission Proteins (Drp And Fis1) Andsupporting

confidence: 86%

“…It is also possible that FIS1 and ELM1 are part of the same mitochondrial membrane complex responsible for recruiting DRP proteins. Lastly, yeast mitochondrial and peroxisomal divisions both require Mdv1p (or Caf4p), a cytosolic linker that interacts with both DRP and FIS1 proteins on these organelles (reviewed in Delille et al, 2009). Although the orthologs for Mdv1p/Caf4p were not identified in mammals, we cannot exclude the possibility that their functional analogs exist in plants.…”

Section: Coordination Between the Fission Proteins (Drp And Fis1) Andmentioning

confidence: 98%

“…Constitutive division and proliferation both involve peroxisome elongation (growth), constriction, and fission and form at least two peroxisomes from a single preexisting peroxisome (Yan et al, 2005;Fagarasanu et al, 2007). Previous studies have identified a number of key factors in peroxisome division/proliferation, among which PEROXIN11 (PEX11), dynamin-related proteins (DRPs), and FISSION1 (FIS1) represent three evolutionarily conserved families of proteins that mediate various stages of division and proliferation (Delille et al, 2009;.…”

Section: Introductionmentioning

confidence: 99%

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The Arabidopsis Chloroplast Division Protein DYNAMIN-RELATED PROTEIN5B Also Mediates Peroxisome Division

Zhang

2010

Plant Cell

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Peroxisomes are highly dynamic organelles involved in various metabolic pathways. The division of peroxisomes is regulated by factors such as the PEROXIN11 (PEX11) proteins that promote peroxisome elongation and the dynamin-related proteins (DRPs) and FISSION1 (FIS1) proteins that function together to mediate organelle fission. In Arabidopsis thaliana, DRP3A/DRP3B and FIS1A (BIGYIN)/FIS1B are two pairs of homologous proteins known to function in both peroxisomal and mitochondrial division. Here, we report that DRP5B, a DRP distantly related to the DRP3s and originally identified as a chloroplast division protein, also contributes to peroxisome division. DRP5B localizes to both peroxisomes and chloroplasts. Mutations in the DRP5B gene lead to peroxisome division defects and compromised peroxisome functions. Using coimmunoprecipitation and bimolecular fluorescence complementation assays, we further demonstrate that DRP5B can interact or form a complex with itself and with DRP3A, DRP3B, FIS1A, and most of the Arabidopsis PEX11 isoforms. Our data suggest that, in contrast with DRP3A and DRP3B, whose orthologs exist across plant, fungal, and animal kingdoms, DRP5B is a plant/algal invention to facilitate the division of their organelles (i.e., chloroplasts and peroxisomes). In addition, our results support the notion that proteins involved in the early (elongation) and late (fission) stages of peroxisome division may act cooperatively.

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Section: Coordination Between the Fission Proteins (Drp And Fis1) Andsupporting

confidence: 86%

Section: Coordination Between the Fission Proteins (Drp And Fis1) Andmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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The Arabidopsis Chloroplast Division Protein DYNAMIN-RELATED PROTEIN5B Also Mediates Peroxisome Division

Zhang

2010

Plant Cell

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“…Sharing of fission components has probably developed by similar cellular demands, as peroxisomes and mitochondria are metabolically linked [13]. This cooperative interaction likely influences the functionality of both organelles in health and disease [14,15]. GDAP1 (ganglioside-induced differentiation associated protein 1) is also a TA-protein of the MOM acting as mitochondrial fission factor [16][17][18].…”

Section: Introductionmentioning

confidence: 99%

Charcot‐Marie‐Tooth disease‐associated mutants of GDAP1 dissociate its roles in peroxisomal and mitochondrial fission

et al. 2013

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Mitochondria and peroxisomes can be fragmented by the process of fission. The fission machineries of both organelles share a set of proteins. GDAP1 is a tail-anchored protein of mitochondria and induces mitochondrial fragmentation. Mutations in GDAP1 lead to Charcot-Marie-Tooth disease (CMT), an inherited peripheral neuropathy, and affect mitochondrial dynamics. Here, we show that GDAP1 is also targeted to peroxisomes mediated by the import receptor Pex19. Knockdown of GDAP1 leads to peroxisomal elongation that can be rescued by re-expressing GDAP1 and by missense mutated forms found in CMT patients. GDAP1-induced peroxisomal fission is dependent on the integrity of its hydrophobic domain 1, and on Drp1 and Mff, as is mitochondrial fission. Thus, GDAP1 regulates mitochondrial and peroxisomal fission by a similar mechanism. However, our results reveal also a more critical role of the amino-terminal GDAP1 domains, carrying most CMT-causing mutations, in the regulation of mitochondrial compared to peroxisomal fission.

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“…Peroxisomes and mitochondria are known to share components of their divisional machineries (Delille et al, 2009). New evidence suggests that peroxisomes and mitochondria also have a common mechanism of distributing themselves between mother cell and bud, which is controlled by their tethering to the ER (Fig.…”

Section: Organelle Division -Integrating Transport and Retentionmentioning

confidence: 99%

Sharing the cell's bounty – organelle inheritance in yeast

Knoblach

Rachubinski

2015

Journal of Cell Science

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Eukaryotic cells replicate and partition their organelles between the mother cell and the daughter cell at cytokinesis. Polarized cells, notably the budding yeast Saccharomyces cerevisiae, are well suited for the study of organelle inheritance, as they facilitate an experimental dissection of organelle transport and retention processes. Much progress has been made in defining the molecular players involved in organelle partitioning in yeast. Each organelle uses a distinct set of factors -motor, anchor and adaptor proteins -that ensures its inheritance by future generations of cells. We propose that all organelles, regardless of origin or copy number, are partitioned by the same fundamental mechanism involving division and segregation. Thus, the mother cell keeps, and the daughter cell receives, their fair and equitable share of organelles. This mechanism of partitioning moreover facilitates the segregation of organelle fragments that are not functionally equivalent. In this Commentary, we describe how this principle of organelle population control affects peroxisomes and other organelles, and outline its implications for yeast life span and rejuvenation.

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Biogenesis of peroxisomes and mitochondria: linked by division

Cited by 63 publications

References 52 publications

The Arabidopsis Chloroplast Division Protein DYNAMIN-RELATED PROTEIN5B Also Mediates Peroxisome Division

The Arabidopsis Chloroplast Division Protein DYNAMIN-RELATED PROTEIN5B Also Mediates Peroxisome Division

Charcot‐Marie‐Tooth disease‐associated mutants of GDAP1 dissociate its roles in peroxisomal and mitochondrial fission

Sharing the cell's bounty – organelle inheritance in yeast

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