Phosphorylation of Pex11p does not regulate peroxisomal fission in the yeast Hansenula polymorpha

Thomas, Ann; Krikken, Arjen M; Klei, Ida J. van der; Williams, Chris P

doi:10.1038/srep11493

Cited by 17 publications

(20 citation statements)

References 23 publications

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“…Beyond those observations there are no congruent reports on the effects of Pex11 phosphorylation: whereas Knoblach and Rachubinski suggested a role of ScPex11 phosphorylation in the formation of peroxisomes from the ER, Joshi and co-workers rather associated PpPex11 phosphorylation with the recruitment of the fission factor Fis1p. Phosphorylation of HpPex11, however, neither influenced peroxisome fission nor Pex11 localization [161]. Currently no elaborate studies on the phosphorylation of mammalian Pex11 exist (note that the homologous residue to yeast, S165/173/174, only appears to be conserved in Pex11α).…”

Section: Towards Understanding Peroxin Phosphorylationmentioning

confidence: 97%

See 1 more Smart Citation

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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Section: Towards Understanding Peroxin Phosphorylationmentioning

confidence: 97%

“…Pex11 phosphorylation was described in the yeast species S. cerevisiae, P. pastoris and H. polymorpha at the homologous position S165/S173/S174, respectively [68,75,161]. Sc and PpPex11 phosphorylation increased under peroxisome proliferating conditions.…”

Section: Towards Understanding Peroxin Phosphorylationmentioning

confidence: 98%

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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“…However, the rapid formation of peroxules in response to ROS would suggest that post-translational modifications of PEX11a could be involved in activating peroxin-promoting peroxules. Although no information is available on PEX11 activation in plants, peroxines Pex11p in yeast has been reported to be activated by protein dimerization, which is regulated by redox changes in cysteines (Knoblach and Rachubinski, 2010;Schrader et al, 2012); however, other post-translational modifications of Pex11p such as phosphorylation are a subject of debate (Thomas et al, 2015). Proteomic studies are required to clarify the rapid regulation of peroxule formation and the role played by the posttranslational modification of PEX11a.…”

Section: Discussionmentioning

confidence: 99%

Peroxisomes Extend Peroxules in a Fast Response to Stress via a Reactive Oxygen Species-Mediated Induction of the Peroxin PEX11a

et al. 2016

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Peroxisomes are highly dynamic and metabolically active organelles that play an important role in cellular functions, including reactive oxygen species (ROS) metabolism. Peroxisomal dynamics, such as the proliferation, movement, and production of dynamic extensions called peroxules, have been associated with ROS in plant cells. However, the function and regulation of peroxules are largely unknown. Using confocal microscopy, we have shown that treatment of Arabidopsis leaves with the heavy metal cadmium produces time course-dependent changes in peroxisomal dynamics, starting with peroxule formation, followed by peroxisome proliferation, and finally returning to the normal morphology and number. These changes during Cd treatment were regulated by NADPH oxidase (C and F)-related ROS production. Peroxule formation is a general response to stimuli such as arsenic and is regulated by peroxin 11a (PEX11a), as Arabidopsis pex11a RNA i lines are unable to produce peroxules under stress conditions. The pex11a line showed higher levels of lipid peroxidation content and lower expression of genes involved in antioxidative defenses and signaling, suggesting that these extensions are involved in regulating ROS accumulation and ROSdependent gene expression in response to stress. Our results demonstrate that PEX11a and peroxule formation play a key role in regulating stress perception and fast cell responses to environmental cues.Peroxisomes are highly versatile organelles that adapt to changes in their cellular environment through morphological and metabolic adjustments (Hu et al., 2012;Sandalio et al., 2013). Plant peroxisomes perform essential functions such as photorespiration and fatty acid b-oxidation, ureide, and phytohormone (auxin and jasmonic acid) metabolisms, and also act as a source of signal molecules such as reactive oxygen and nitrogen species (ROS and RNS; Sandalio and RomeroPuertas, 2015). Peroxisomes contain a large battery of antioxidants to control ROS and RNS accumulation (Sandalio and Romero-Puertas, 2015). These organelles proliferate in response to environmental cues through a complex process involving elongation, constriction, and fission (Hu et al., 2012;Baker and Paudyal, 2014). Deciphering the signaling pathways governing the regulation of peroxisome proliferation under different environmental and metabolic conditions presents a major challenge in this field of research. Before peroxisomal division, organelle elongation occurs in a process regulated by peroxins 11 (PEX11), with the final division requiring dynamin-like or dynamin-related proteins and fission proteins (Hu et al., 2012, Schrader et al., 2012. There is evidence to suggest that ROS are involved in regulating peroxisome proliferation, as some peroxisomal biogenesis genes (PEX) are transcriptionally regulated by H 2 O 2 in both plant and animal cells (López-Huertas et al., 2000). The formation of peroxisomal extensions, known as peroxules, has also been observed to be regulated by exogenous applications of H 2 O 2 (Sinclair et al., 2009;Ba...

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“…Next, we quantified the number of GFP containing spots by confocal laser scanning microscopy (CLSM) and a custom-made plugin for ImageJ (Thomas et al, 2015). In these images cytosolic fluorescence was not detected in any of the strains due to the lower sensitivity of CLSM relative to wide field FM.…”

Section: Pex24 and Pex32 Are Important For Peroxisome Biogenesis And mentioning

confidence: 99%

“…To test whether the Pex24/Pex32 dependent ER-peroxisome contacts are important for expansion of peroxisomal membranes, we compared the average peroxisomal membrane surface per cell in the four deletion strains relative to the WT control. The plug-in for the analysis of CLSM images allows quantifying the average diameter of peroxisomes by fitting spheres in data obtained from the green channel of combined z-slices of glycerol/methanol grown, PMP47-GFP 17 producing cells (Thomas et al, 2015). From these data we estimated the average peroxisomal membrane surface per cell.…”

Section: An Artificial Er-peroxisome Tether Suppresses the Peroxisomamentioning

confidence: 99%

Pex24 and Pex32 tether peroxisomes to the ER for organelle biogenesis, positioning and segregation

Wu¹,

Boer²,

Krikken³

et al. 2020

Preprint

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Two Hansenula polymorpha ER proteins, Pex24 and Pex32, are tethers at peroxisome-ER contacts and function together with the peroxisomal protein Pex11. Their absence disturbs these contacts leading to multiple peroxisomal defects, which can be restored by an artificial tether. AbstractWe analyzed all four Pex23 family proteins of the yeast Hansenula polymorpha, which localize to the ER. Of these Pex24 and Pex32, but not Pex23 and Pex29, accumulate at peroxisome-ER contacts, where they are important for normal peroxisome biogenesis and proliferation and contribute to organelle positioning and segregation.Upon deletion of PEX24 and PEX32 -and to a lesser extent of PEX23 and PEX29peroxisome-ER contacts are disrupted, concomitant with peroxisomal defects. These defects are suppressed upon introduction of an artificial peroxisome-ER tether.

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Phosphorylation of Pex11p does not regulate peroxisomal fission in the yeast Hansenula polymorpha

Cited by 17 publications

References 23 publications

Proliferation and fission of peroxisomes — An update

Proliferation and fission of peroxisomes — An update

Peroxisomes Extend Peroxules in a Fast Response to Stress via a Reactive Oxygen Species-Mediated Induction of the Peroxin PEX11a

Pex24 and Pex32 tether peroxisomes to the ER for organelle biogenesis, positioning and segregation

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