Signaling dynamics and peroxisomes

Mast, Fred D.; Rachubinski, Richard A.; Aitchison, John D.

doi:10.1016/j.ceb.2015.05.002

Cited by 32 publications

(21 citation statements)

References 47 publications

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“…Because these metabolic parameters were determined at a final stage of liver regeneration (2 weeks post‐PH), we hypothesize that increased reduced nicotinamide adenine dinucleotide phosphate generated in the PPC is also being used for detoxification against the massive damage occurring after PH that, in addition to glucose availability, likely contributed to decreased PLF. These data were also supported by the up‐regulation of peroxisome metabolism family genes and by the increased number of peroxisomes, organelles responsible for the detoxification of dangerous reactive oxygen species . In addition, a marked antioxidant effect of G49 was found after PH that may result from its ability to increase both antioxidant enzymes and GSH levels.…”

Section: Discussionsupporting

confidence: 77%

“…These data were also supported by the up-regulation of peroxisome metabolism family genes and by the increased number of peroxisomes, organelles responsible for the detoxification of dangerous reactive oxygen species. (46) In addition, a marked antioxidant effect of G49 was found after PH that may result from its ability to increase both antioxidant enzymes and GSH levels.…”

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confidence: 99%

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A novel glucagon‐like peptide 1/glucagon receptor dual agonist improves steatohepatitis and liver regeneration in mice

et al. 2017

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Section: Discussionsupporting

confidence: 77%

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confidence: 99%

A novel glucagon‐like peptide 1/glucagon receptor dual agonist improves steatohepatitis and liver regeneration in mice

et al. 2017

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“…To perform their multiple metabolic tasks, peroxisomes cooperate with several other subcellular compartments including mitochondria, ER, lipid droplets or lysosomes [25,140,142]. In addition, peroxisomes represent important intracellular signalling platforms in redox-, lipid-, inflammatory-, and antiviral signalling [100,112,115]. As dynamic organelles, peroxisomes have the capability to proliferate in response to environmental stimuli and are degraded to maintain default numbers when the stimuli dissipate.…”

Section: Introductionmentioning

confidence: 99%

Proliferation and fission of peroxisomes — An update

Schrader

Costello

Godinho

et al. 2016

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

123

142

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In mammals, peroxisomes perform crucial functions in cellular metabolism, signalling and viral defense which are essential to the health and viability of the organism. In order to achieve this functional versatility peroxisomes dynamically respond to molecular cues triggered by changes in the cellular environment. Such changes elicit a corresponding response in peroxisomes, which manifests itself as a change in peroxisome number, altered enzyme levels and adaptations to the peroxisomal structure. In mammals the generation of new peroxisomes is a complex process which has clear analogies to mitochondria, with both sharing the same division machinery and undergoing a similar division process. How the regulation of this division process is integrated into the cell's response to different stimuli, the signalling pathways and factors involved, remains somewhat unclear. Here, we discuss the mechanism of peroxisomal fission, the contributions of the various division factors and examine the potential impact of post-translational modifications, such as phosphorylation, on the proliferation process. We also summarize the signalling process and highlight the most recent data linking signalling pathways with peroxisome proliferation.

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“…Control of these processes is critical to human health. Defects in peroxisome membrane formation, protein import, and organelle proliferation cause severe pathologies in humans, and peroxisome function is linked to numerous human health issues (1)(2)(3)(4). Studies in many different model systems, including notably different species of yeast, have led to the identification of peroxins, which are defined as proteins involved in peroxisome biogenesis (5).…”

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confidence: 99%

Peroxins Pex30 and Pex29 Dynamically Associate with Reticulons to Regulate Peroxisome Biogenesis from the Endoplasmic Reticulum

Mast

Jamakhandi

Saleem

et al. 2016

Journal of Biological Chemistry

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Peroxisome proliferation occurs by at least two routes, division of existing peroxisomes and de novo biogenesis from the endoplasmic reticulum (ER). The proteins and molecular mechanisms governing peroxisome emergence from the ER are poorly characterized. In this study, we report that two integral membrane peroxins (proteins required for peroxisome biogenesis) in Saccharomyces cerevisiae, Pex29 and Pex30, reside in distinct regions of the ER and associate with Rtn1 and Yop1, reticulon family members that contribute to ER morphology, to govern peroxisome emergence from the ER. In vivo and in vitro analyses reveal that peroxisome proliferation is therefore not restricted to the peroxisome but begins at the level of the ER.Peroxisomes are organelles found across the diversity of eukaryotes. Bound by a single lipid bilayer, peroxisomes contain enzymes involved in lipid metabolism that are coupled to the production of hydrogen peroxide and the scavenging of reactive oxygen species. Peroxisome number, size, and volume are dynamically linked to cell type, its developmental state, and environmental stimuli. Control of these processes is critical to human health. Defects in peroxisome membrane formation, protein import, and organelle proliferation cause severe pathologies in humans, and peroxisome function is linked to numerous human health issues (1-4). Studies in many different model systems, including notably different species of yeast, have led to the identification of peroxins, which are defined as proteins involved in peroxisome biogenesis (5). The mechanisms of action of the more than 30 peroxins in peroxisomal biogenesis and proliferation are the subject of intense investigation.There has been much debate as to whether peroxisomes are semi-autonomous organelles like mitochondria or are derived from internal membrane systems such as the secretory pathway. Evidence supports that peroxisome biogenesis occurs through two separate pathways, de novo biogenesis in which new peroxisomes bud from the ER 3 and the division of existing peroxisomes (6 -12). These biogenesis pathways are tightly regulated spatially and temporally and involve a host of molecular interactions that mediate the assembly of proteins and lipids at the peroxisome membrane and the ER (13-16). In the budding yeast Saccharomyces cerevisiae, growth and division of peroxisomes are the dominant forms of peroxisome proliferation. However, contribution from the ER is an essential albeit poorly understood process. When peroxisomes are absent, cells form peroxisomes de novo from the ER. Presumably, interactions between proteins and lipids at the ER result in de novo biogenesis of nascent preperoxisomes that undergo a series of steps to ultimately form mature peroxisomes. Several peroxisomal membrane proteins (PMPs) insert into the ER dependent on components of the Sec61 complex, and the subsequent formation of preperoxisomes is dependent on the peroxins Pex3 and Pex19. Pex3 is an integral membrane protein that accumulates initially at an ER subdomain and is t...

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Signaling dynamics and peroxisomes

Cited by 32 publications

References 47 publications

A novel glucagon‐like peptide 1/glucagon receptor dual agonist improves steatohepatitis and liver regeneration in mice

A novel glucagon‐like peptide 1/glucagon receptor dual agonist improves steatohepatitis and liver regeneration in mice

Proliferation and fission of peroxisomes — An update

Peroxins Pex30 and Pex29 Dynamically Associate with Reticulons to Regulate Peroxisome Biogenesis from the Endoplasmic Reticulum

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