Comparative Genomics of Peroxisome Biogenesis Proteins: Making Sense of the PEX Proteins

Jansen, Renate; Santana-Molina, Carlos; Noort, Marco van den; Devos, Damien P.; Klei, Ida J. van der

doi:10.3389/fcell.2021.654163

Cited by 56 publications

(70 citation statements)

References 119 publications

(187 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…PMPs can also sort directly to the membranes of peroxisomes (Mayerhofer, 2016). The homologs of the Pex23 and Pex24 family of peroxins in various yeasts (Figure 1) that reside in the ER membrane play an important role at peroxisome-ER contact sites (Yan et al, 2008;David et al, 2013;Mast et al, 2016;Wu et al, 2020;Ferreira and Carvalho, 2021;Jansen et al, 2021). In S. cerevisiae, ScPex29 and ScPex30, whereas in O. polymorpha, OpPex24 and OpPex32 accumulate at the peroxisome-ER MCS (David et al, 2013;Mast et al, 2016) (Figure 1).…”

Section: Peroxisome-er Contact Sitesmentioning

confidence: 99%

Peroxisomal Membrane Contact Sites in Yeasts

Joshi

2021

Front. Cell Dev. Biol.

View full text Add to dashboard Cite

Peroxisomes are ubiquitous, single membrane-bound organelles that play a crucial role in lipid metabolism and human health. While peroxisome number is maintained by the division of existing peroxisomes, nascent peroxisomes can be generated from the endoplasmic reticulum (ER) membrane in yeasts. During formation and proliferation, peroxisomes maintain membrane contacts with the ER. In addition to the ER, contacts between peroxisomes and other organelles such as lipid droplets, mitochondria, vacuole, and plasma membrane have been reported. These membrane contact sites (MCS) are dynamic and important for cellular function. This review focuses on the recent developments in peroxisome biogenesis and the functional importance of peroxisomal MCS in yeasts.

show abstract

Section: Peroxisome-er Contact Sitesmentioning

confidence: 99%

Peroxisomal Membrane Contact Sites in Yeasts

Joshi

2021

Front. Cell Dev. Biol.

View full text Add to dashboard Cite

show abstract

“…Our data indicate that H. polymorpha Vps13 functions together with Pex23 and Pex24 in peroxisomal membrane expansion. Like other protein of the Pex23 family, Pex23 and Pex24 contain a dysferlin (DysF) domain ( Jansen et al, 2021 ). DysF was first identified in dysferlin, a human protein important for membrane repair of the sarcolemma at the site of muscle injury.…”

Section: Discussionmentioning

confidence: 99%

“…ER-localized peroxins of the Pex23 family (Pex23, Pex24 and Pex32) together with the peroxisomal membrane protein (PMP) Pex11 play a role in the formation of peroxisome-ER contacts ( Wu et al, 2020 ). Similarly, members of the S. cerevisiae Pex23 family (called Pex28, Pex29, Pex30, Pex31 and Pex32 ( Jansen et al, 2021 )) have been implicated in the formation of peroxisome ER contact sites ( David et al, 2013 ; Mast et al, 2016 ). S. cerevisiae Pex23 family proteins also have been implicated in other processes, such as the regulation of pre-peroxisomal vesicle (PPV) formation from the ER ( David et al, 2013 ; Joshi et al, 2016 ; Mast et al, 2016 ; Wang et al, 2018 ) and the biogenesis of lipid bodies ( Joshi et al, 2018 ).…”

Section: Introductionmentioning

confidence: 99%

Yeast Vps13 is Crucial for Peroxisome Expansion in Cells With Reduced Peroxisome-ER Contact Sites

Yuan

Akşit

Boer

et al. 2022

Front. Cell Dev. Biol.

Self Cite

View full text Add to dashboard Cite

In the yeast Hansenula polymorpha the peroxisomal membrane protein Pex11 and three endoplasmic reticulum localized proteins of the Pex23 family (Pex23, Pex24 and Pex32) are involved in the formation of peroxisome-ER contact sites. Previous studies suggested that these contacts are involved in non-vesicular lipid transfer and important for expansion of the peroxisomal membrane. The absence of Pex32 results in a severe peroxisomal phenotype, while cells lacking Pex11, Pex23 or Pex24 show milder defects and still are capable to form peroxisomes and grow on methanol. We performed transposon mutagenesis on H. polymorpha pex11 cells and selected mutants that lost the capacity to grow on methanol and are severely blocked in peroxisome formation. This strategy resulted in the identification of Vps13, a highly conserved contact site protein involved in bulk lipid transfer. Our data show that peroxisome formation and function is normal in cells of a vps13 single deletion strain. However, Vps13 is essential for peroxisome biogenesis in pex11. Notably, Vps13 is also required for peroxisome formation in pex23 and pex24 cells. These data suggest that Vps13 is crucial for peroxisome formation in cells with reduced peroxisome-endoplasmic reticulum contact sites and plays a redundant function in lipid transfer from the ER to peroxisomes.

show abstract

“…29 Consistent with the downregulation of PEX3, peroxisome marker PEX14, a component of the receptor docking site, was decreased in the MHF fetus. PEX5/7, matrix protein receptor, and PEX1,6 and 26, involved in receptor recycling, 30 were all upregulated. These findings are valuable for the further study of impact of excess fatty acids on peroxisome biogenesis in renal tubular cells.…”

Section: Discussionmentioning

confidence: 99%

Maternal High-Fat Diet Programs Renal Peroxisomes and Activates NLRP3 Inflammasome-Mediated Pyroptosis in the Rat Fetus

Zhou¹,

Guan²,

Guo³

et al. 2021

JIR

View full text Add to dashboard Cite

Maternal obesity impairs kidney development and function of the offspring and leads to a greater risk of kidney disease in adulthood. The present study aimed to investigate the link between peroxisomes, oxidative stress (OS), and inflammasomes in the fetal kidney of maternal obesity rats and to explore the potential therapeutic effects of the antioxidant pyrroloquinoline quinone (PQQ). Methods: Maternal obesity rats were developed by administration of a high fat diet plus supplementation with PQQ (40 mg/kg body weight) as a potential therapy. Renal histology was observed by Periodic Acid-Schiff staining. The expression profiles of peroxins, fatty acid β-oxidation enzymes, antioxidants, and the regulators of the unfolded protein response (UPR) pathway and NLRP3 inflammasome were analyzed in the kidneys and tubular epithelial cells (TECs) from near-term fetuses (embryonic day 20). Results: The present work revealed that: 1) a maternal high fat diet (MHF) led to higher blood pressure in adult offspring; 2) MHF led to downregulation of peroxisome markers PEX3 and 14 in fetal kidneys; 3) the antioxidant SOD2 and catalase were decreased, and oxidative stress marker Ephx2 was increased; 4) MHF-induced activation of the UPR pathway; 5) the KEAP1-NRF2 pathway was activated; 6) activation of the NLRP3 inflammasome led to secretion of pro-inflammation factors; 7) in TECs, the changes in PEXs and NLRP3 are similar to tissues, but UPR and NRF2 pathways showed opposite trends; 8) and the antioxidant PQQ alleviated maternal lipotoxicity by decreasing ROS levels and inhibiting activation of ER stress and inflammasome in fetal kidney. Conclusion:A maternal high fat diet decreased the number of peroxisomes, subsequently activated OS and inflammasomes, resulting in pyroptosis and apoptosis in fetal kidney. The antioxidant PQQ served a protective role against the effects of lipotoxicity on kidney programming and, thus, is a potential candidate to prevent maternal obesity-induced renal programming.

show abstract

Comparative Genomics of Peroxisome Biogenesis Proteins: Making Sense of the PEX Proteins

Cited by 56 publications

References 119 publications

Peroxisomal Membrane Contact Sites in Yeasts

Peroxisomal Membrane Contact Sites in Yeasts

Yeast Vps13 is Crucial for Peroxisome Expansion in Cells With Reduced Peroxisome-ER Contact Sites

Maternal High-Fat Diet Programs Renal Peroxisomes and Activates NLRP3 Inflammasome-Mediated Pyroptosis in the Rat Fetus

Contact Info

Product

Resources

About