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Artículos de revistas sobre el tema "PEX1"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 20 de febrero de 2023

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1

Knoops, Kèvin, Rinse de Boer, Anita Kram, and Ida J. van der Klei. "Yeast pex1 cells contain peroxisomal ghosts that import matrix proteins upon reintroduction of Pex1." Journal of Cell Biology 211, no. 5 (December 7, 2015): 955–62. http://dx.doi.org/10.1083/jcb.201506059.

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Pex1 and Pex6 are two AAA-ATPases that play a crucial role in peroxisome biogenesis. We have characterized the ultrastructure of the Saccharomyces cerevisiae peroxisome-deficient mutants pex1 and pex6 by various high-resolution electron microscopy techniques. We observed that the cells contained peroxisomal membrane remnants, which in ultrathin cross sections generally appeared as double membrane rings. Electron tomography revealed that these structures consisted of one continuous membrane, representing an empty, flattened vesicle, which folds into a cup shape. Immunocytochemistry revealed tha

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2

Verner, Zdeněk, Vojtěch Žárský, Tien Le, Ravi Kumar Narayanasamy, Petr Rada, Daniel Rozbeský, Abhijith Makki, et al. "Anaerobic peroxisomes in Entamoeba histolytica metabolize myo-inositol." PLOS Pathogens 17, no. 11 (November 15, 2021): e1010041. http://dx.doi.org/10.1371/journal.ppat.1010041.

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Entamoeba histolytica is believed to be devoid of peroxisomes, like most anaerobic protists. In this work, we provided the first evidence that peroxisomes are present in E. histolytica, although only seven proteins responsible for peroxisome biogenesis (peroxins) were identified (Pex1, Pex6, Pex5, Pex11, Pex14, Pex16, and Pex19). Targeting matrix proteins to peroxisomes is reduced to the PTS1-dependent pathway mediated via the soluble Pex5 receptor, while the PTS2 receptor Pex7 is absent. Immunofluorescence microscopy showed that peroxisomal markers (Pex5, Pex14, Pex16, Pex19) are present in v

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3

Agrawal, Gaurav, Scott N. Fassas, Zhi-Jie Xia, and Suresh Subramani. "Distinct requirements for intra-ER sorting and budding of peroxisomal membrane proteins from the ER." Journal of Cell Biology 212, no. 3 (February 1, 2016): 335–48. http://dx.doi.org/10.1083/jcb.201506141.

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During de novo peroxisome biogenesis, importomer complex proteins sort via two preperoxisomal vesicles (ppVs). However, the sorting mechanisms segregating peroxisomal membrane proteins to the preperoxisomal endoplasmic reticulum (pER) and into ppVs are unknown. We report novel roles for Pex3 and Pex19 in intra–endoplasmic reticulum (ER) sorting and budding of the RING-domain peroxins (Pex2, Pex10, and Pex12). Pex19 bridged the interaction at the ER between Pex3 and RING-domain proteins, resulting in a ternary complex that was critical for the intra-ER sorting and subsequent budding of the RING

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4

Miyata, Non, and Yukio Fujiki. "Shuttling Mechanism of Peroxisome Targeting Signal Type 1 Receptor Pex5: ATP-Independent Import and ATP-Dependent Export." Molecular and Cellular Biology 25, no. 24 (December 15, 2005): 10822–32. http://dx.doi.org/10.1128/mcb.25.24.10822-10832.2005.

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ABSTRACT Peroxisomal matrix proteins are posttranslationally imported into peroxisomes with the peroxisome-targeting signal 1 receptor, Pex5. The longer isoform of Pex5, Pex5L, also transports Pex7-PTS2 protein complexes. After unloading the cargoes, Pex5 returns to the cytosol. To address molecular mechanisms underlying Pex5 functions, we constructed a cell-free Pex5 translocation system with a postnuclear supernatant fraction from CHO cell lines. In assays using the wild-type CHO-K1 cell fraction, 35S-labeled Pex5 was specifically imported into and exported from peroxisomes with multiple rou

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5

Gonzalez, Kim L., Sarah E. Ratzel, Kendall H. Burks, Charles H. Danan, Jeanne M. Wages, Bethany K. Zolman, and Bonnie Bartel. "A pex1 missense mutation improves peroxisome function in a subset of Arabidopsis pex6 mutants without restoring PEX5 recycling." Proceedings of the National Academy of Sciences 115, no. 14 (March 19, 2018): E3163—E3172. http://dx.doi.org/10.1073/pnas.1721279115.

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Peroxisomes are eukaryotic organelles critical for plant and human development because they house essential metabolic functions, such as fatty acid β-oxidation. The interacting ATPases PEX1 and PEX6 contribute to peroxisome function by recycling PEX5, a cytosolic receptor needed to import proteins targeted to the peroxisomal matrix. Arabidopsis pex6 mutants exhibit low PEX5 levels and defects in peroxisomal matrix protein import, oil body utilization, peroxisomal metabolism, and seedling growth. These defects are hypothesized to stem from impaired PEX5 retrotranslocation leading to PEX5 polyub

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6

Titorenko, V. I., D. M. Ogrydziak, and R. A. Rachubinski. "Four distinct secretory pathways serve protein secretion, cell surface growth, and peroxisome biogenesis in the yeast Yarrowia lipolytica." Molecular and Cellular Biology 17, no. 9 (September 1997): 5210–26. http://dx.doi.org/10.1128/mcb.17.9.5210.

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We have identified and characterized mutants of the yeast Yarrowia lipolytica that are deficient in protein secretion, in the ability to undergo dimorphic transition from the yeast to the mycelial form, and in peroxisome biogenesis. Mutations in the SEC238, SRP54, PEX1, PEX2, PEX6, and PEX9 genes affect protein secretion, prevent the exit of the precursor form of alkaline extracellular protease from the endoplasmic reticulum, and compromise peroxisome biogenesis. The mutants sec238A, srp54KO, pex2KO, pex6KO, and pex9KO are also deficient in the dimorphic transition from the yeast to the myceli

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7

Chang, C. C., S. South, D. Warren, J. Jones, A. B. Moser, H. W. Moser, and S. J. Gould. "Metabolic control of peroxisome abundance." Journal of Cell Science 112, no. 10 (May 15, 1999): 1579–90. http://dx.doi.org/10.1242/jcs.112.10.1579.

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Zellweger syndrome and related disorders represent a group of lethal, genetically heterogeneous diseases. These peroxisome biogenesis disorders (PBDs) are characterized by defective peroxisomal matrix protein import and comprise at least 10 complementation groups. The genes defective in seven of these groups and more than 90% of PBD patients are now known. Here we examine the distribution of peroxisomal membrane proteins in fibroblasts from PBD patients representing the seven complementation groups for which the mutant gene is known. Peroxisomes were detected in all PBD cells, indicating that

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8

Knoops, Kèvin, Selvambigai Manivannan, Małgorzata N. Cepińska, Arjen M. Krikken, Anita M. Kram, Marten Veenhuis, and Ida J. van der Klei. "Preperoxisomal vesicles can form in the absence of Pex3." Journal of Cell Biology 204, no. 5 (March 3, 2014): 659–68. http://dx.doi.org/10.1083/jcb.201310148.

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We demonstrate that the peroxin Pex3 is not required for the formation of peroxisomal membrane structures in yeast pex3 mutant cells. Notably, pex3 mutant cells already contain reticular and vesicular structures that harbor key proteins of the peroxisomal receptor docking complex—Pex13 and Pex14—as well as the matrix proteins Pex8 and alcohol oxidase. Other peroxisomal membrane proteins in these cells are unstable and transiently localized to the cytosol (Pex10, Pmp47) or endoplasmic reticulum (Pex11). These reticular and vesicular structures are more abundant in cells of a pex3 atg1 double de

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9

Platta, Harald W., Fouzi El Magraoui, Bastian E. Bäumer, Daniel Schlee, Wolfgang Girzalsky, and Ralf Erdmann. "Pex2 and Pex12 Function as Protein-Ubiquitin Ligases in Peroxisomal Protein Import." Molecular and Cellular Biology 29, no. 20 (August 17, 2009): 5505–16. http://dx.doi.org/10.1128/mcb.00388-09.

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ABSTRACT The PTS1-dependent peroxisomal matrix protein import is facilitated by the receptor protein Pex5 and can be divided into cargo recognition in the cytosol, membrane docking of the cargo-receptor complex, cargo release, and recycling of the receptor. The final step is controlled by the ubiquitination status of Pex5. While polyubiquitinated Pex5 is degraded by the proteasome, monoubiquitinated Pex5 is destined for a new round of the receptor cycle. Recently, the ubiquitin-conjugating enzymes involved in Pex5 ubiquitination were identified as Ubc4 and Pex4 (Ubc10), whereas the identity of

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10

Judy, Ryan M., Connor J. Sheedy, and Brooke M. Gardner. "Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis." Cells 11, no. 13 (June 29, 2022): 2067. http://dx.doi.org/10.3390/cells11132067.

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The AAA-ATPases Pex1 and Pex6 are required for the formation and maintenance of peroxisomes, membrane-bound organelles that harbor enzymes for specialized metabolism. Together, Pex1 and Pex6 form a heterohexameric AAA-ATPase capable of unfolding substrate proteins via processive threading through a central pore. Here, we review the proposed roles for Pex1/Pex6 in peroxisome biogenesis and degradation, discussing how the unfolding of potential substrates contributes to peroxisome homeostasis. We also consider how advances in cryo-EM, computational structure prediction, and mechanisms of related

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11

Motley, Alison M., Paul C. Galvin, Lakhan Ekal, James M. Nuttall, and Ewald H. Hettema. "Reevaluation of the role of Pex1 and dynamin-related proteins in peroxisome membrane biogenesis." Journal of Cell Biology 211, no. 5 (December 7, 2015): 1041–56. http://dx.doi.org/10.1083/jcb.201412066.

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A recent model for peroxisome biogenesis postulates that peroxisomes form de novo continuously in wild-type cells by heterotypic fusion of endoplasmic reticulum–derived vesicles containing distinct sets of peroxisomal membrane proteins. This model proposes a role in vesicle fusion for the Pex1/Pex6 complex, which has an established role in matrix protein import. The growth and division model proposes that peroxisomes derive from existing peroxisomes. We tested these models by reexamining the role of Pex1/Pex6 and dynamin-related proteins in peroxisome biogenesis. We found that induced depletio

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12

Blok, Neil B., Dongyan Tan, Ray Yu-Ruei Wang, Pawel A. Penczek, David Baker, Frank DiMaio, Tom A. Rapoport, and Thomas Walz. "Unique double-ring structure of the peroxisomal Pex1/Pex6 ATPase complex revealed by cryo-electron microscopy." Proceedings of the National Academy of Sciences 112, no. 30 (July 13, 2015): E4017—E4025. http://dx.doi.org/10.1073/pnas.1500257112.

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Members of the AAA family of ATPases assemble into hexameric double rings and perform vital functions, yet their molecular mechanisms remain poorly understood. Here, we report structures of the Pex1/Pex6 complex; mutations in these proteins frequently cause peroxisomal diseases. The structures were determined in the presence of different nucleotides by cryo-electron microscopy. Models were generated using a computational approach that combines Monte Carlo placement of structurally homologous domains into density maps with energy minimization and refinement protocols. Pex1 and Pex6 alternate in

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13

Idnurm, Alexander, Steven S. Giles, John R. Perfect, and Joseph Heitman. "Peroxisome Function Regulates Growth on Glucose in the Basidiomycete Fungus Cryptococcus neoformans." Eukaryotic Cell 6, no. 1 (October 13, 2006): 60–72. http://dx.doi.org/10.1128/ec.00214-06.

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ABSTRACT The function of the peroxisomes was examined in the pathogenic basidiomycete Cryptococcus neoformans. Recent studies reveal the glyoxylate pathway is required for virulence of diverse microbial pathogens of plants and animals. One exception is C. neoformans, in which isocitrate lyase (encoded by ICL1) was previously shown not to be required for virulence, and here this was extended to exclude also a role for malate synthase (encoded by MLS1). The role of peroxisomes, in which the glyoxylate pathway enzymes are localized in many organisms, was examined by mutation of two genes (PEX1 an

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14

Schell-Steven, Annette, Katharina Stein, Mara Amoros, Christiane Landgraf, Rudolf Volkmer-Engert, Hanspeter Rottensteiner, and Ralf Erdmann. "Identification of a Novel, Intraperoxisomal Pex14-Binding Site in Pex13: Association of Pex13 with the Docking Complex Is Essential for Peroxisomal Matrix Protein Import." Molecular and Cellular Biology 25, no. 8 (April 15, 2005): 3007–18. http://dx.doi.org/10.1128/mcb.25.8.3007-3018.2005.

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ABSTRACT The peroxisomal docking complex is a key component of the import machinery for matrix proteins. The core protein of this complex, Pex14, is thought to represent the initial docking site for the import receptors Pex5 and Pex7. Associated with this complex is a fraction of Pex13, another essential component of the import machinery. Here we demonstrate that Pex13 directly binds Pex14 not only via its SH3 domain but also via a novel intraperoxisomal site. Furthermore, we demonstrate that Pex5 also contributes to the association of Pex13 with Pex14. Peroxisome function was affected only mi

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15

Havali, Cengiz, Sevil Dorum, Yılmaz Akbaş, Orhan Görükmez, and Tugba Hirfanoglu. "Two different missense mutations of PEX genes in two similar patients with severe Zellweger syndrome: an argument on the genotype-phenotype correlation." Journal of Pediatric Endocrinology and Metabolism 33, no. 3 (March 26, 2020): 437–41. http://dx.doi.org/10.1515/jpem-2019-0194.

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AbstractBackgroundPeroxisomal biogenesis disorders (PBDs) include a miscellaneous group of diseases which cause serious multisystem disease. Mutations of 13 different PEX genes lead to PBDs including Zellweger syndrome (ZS). Different types of mutations of PEX1 and PEX10 genes are correlated with broad-range phenotypes of PBDs.Case presentationPatient 1 is a 4-month-old boy who was affected by myoclonic seizures, poor oral feeding since birth. The patient was hypotonic and had hepatosplenomegaly. Patient 2 is a 2-month-old boy who presented with decreased movement, severe hypotonia and failure

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Schieferdecker, Anne, and Petra Wendler. "Structural Mapping of Missense Mutations in the Pex1/Pex6 Complex." International Journal of Molecular Sciences 20, no. 15 (August 1, 2019): 3756. http://dx.doi.org/10.3390/ijms20153756.

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Peroxisome biogenesis disorders (PBDs) are nontreatable hereditary diseases with a broad range of severity. Approximately 65% of patients are affected by mutations in the peroxins Pex1 and Pex6. The proteins form the heteromeric Pex1/Pex6 complex, which is important for protein import into peroxisomes. To date, no structural data are available for this AAA+ ATPase complex. However, a wealth of information can be transferred from low-resolution structures of the yeast scPex1/scPex6 complex and homologous, well-characterized AAA+ ATPases. We review the abundant records of missense mutations desc

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17

Collins, Cynthia S., Jennifer E. Kalish, James C. Morrell, J. Michael McCaffery, and Stephen J. Gould. "The Peroxisome Biogenesis Factors Pex4p, Pex22p, Pex1p, and Pex6p Act in the Terminal Steps of Peroxisomal Matrix Protein Import." Molecular and Cellular Biology 20, no. 20 (October 15, 2000): 7516–26. http://dx.doi.org/10.1128/mcb.20.20.7516-7526.2000.

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ABSTRACT Peroxisomes are independent organelles found in virtually all eukaryotic cells. Genetic studies have identified more than 20PEX genes that are required for peroxisome biogenesis. The role of most PEX gene products, peroxins, remains to be determined, but a variety of studies have established that Pex5p binds the type 1 peroxisomal targeting signal and is the import receptor for most newly synthesized peroxisomal matrix proteins. The steady-state abundance of Pex5p is unaffected in mostpex mutants of the yeast Pichia pastorisbut is severely reduced in pex4 andpex22 mutants and moderate

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Nuttall, James M., Alison M. Motley, and Ewald H. Hettema. "Deficiency of the exportomer components Pex1, Pex6, and Pex15 causes enhanced pexophagy inSaccharomyces cerevisiae." Autophagy 10, no. 5 (March 18, 2014): 835–45. http://dx.doi.org/10.4161/auto.28259.

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Fujiki, Yukio, Non Miyata, Naomi Matsumoto, and Shigehiko Tamura. "Dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p involved in shuttling of the PTS1 receptor Pex5p in peroxisome biogenesis." Biochemical Society Transactions 36, no. 1 (January 22, 2008): 109–13. http://dx.doi.org/10.1042/bst0360109.

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The peroxisome is a single-membrane-bound organelle found in eukaryotes. The functional importance of peroxisomes in humans is highlighted by peroxisome-deficient PBDs (peroxisome biogenesis disorders), such as Zellweger syndrome. Two AAA (ATPase associated with various cellular activities) peroxins, Pex1p and Pex6p, are encoded by PEX1 and PEX6, the causal genes for CG (complementation group) 1 and CG4 PBDs respectively. PEX26, which is responsible for CG8 PBDs, codes for Pex26p, the recruiter of Pex1p–Pex6p complexes to peroxisomes. We recently assigned the binding regions between human Pex1

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Smith, Claire E. L., James A. Poulter, Alex V. Levin, Jenina E. Capasso, Susan Price, Tamar Ben-Yosef, Reuven Sharony, et al. "Spectrum of PEX1 and PEX6 variants in Heimler syndrome." European Journal of Human Genetics 24, no. 11 (June 15, 2016): 1565–71. http://dx.doi.org/10.1038/ejhg.2016.62.

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Chang, Chia-Che, Daniel S. Warren, Katherine A. Sacksteder, and Stephen J. Gould. "Pex12 Interacts with Pex5 and Pex10 and Acts Downstream of Receptor Docking in Peroxisomal Matrix Protein Import." Journal of Cell Biology 147, no. 4 (November 15, 1999): 761–74. http://dx.doi.org/10.1083/jcb.147.4.761.

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Peroxisomal matrix protein import requires PEX12, an integral peroxisomal membrane protein with a zinc ring domain at its carboxy terminus. Mutations in human PEX12 result in Zellweger syndrome, a lethal neurological disorder, and implicate the zinc ring domain in PEX12 function. Using two-hybrid studies, blot overlay assays, and coimmunoprecipitation experiments, we observed that the zinc-binding domain of PEX12 binds both PEX5, the PTS1 receptor, and PEX10, another integral peroxisomal membrane protein required for peroxisomal matrix protein import. Furthermore, we identified a patient with

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TAMURA, Shigehiko, Naomi MATSUMOTO, Atsushi IMAMURA, Nobuyuki SHIMOZAWA, Yasuyuki SUZUKI, Naomi KONDO, and Yukio FUJIKI. "Phenotype–genotype relationships in peroxisome biogenesis disorders of PEX1-defective complementation group 1 are defined by Pex1p–Pex6p interaction." Biochemical Journal 357, no. 2 (July 9, 2001): 417–26. http://dx.doi.org/10.1042/bj3570417.

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The peroxisome biogenesis disorders (PBDs), including Zellweger syndrome (ZS), neonatal adrenoleucodystrophy (NALD) and infantile Refsum disease (IRD), are fatal autosomal recessive diseases caused by impaired peroxisome biogenesis, of which 12 genotypes have been reported. ZS patients manifest the severest clinical and biochemical abnormalities, whereas those with NALD and IRD show less severity and the mildest features respectively. We have reported previously that temperature-sensitive peroxisome assembly is responsible for the mildness of the clinical features of IRD. PEX1 is the causative

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Titorenko, Vladimir I., and Richard A. Rachubinski. "Mutants of the Yeast Yarrowia lipolyticaDefective in Protein Exit from the Endoplasmic Reticulum Are Also Defective in Peroxisome Biogenesis." Molecular and Cellular Biology 18, no. 5 (May 1, 1998): 2789–803. http://dx.doi.org/10.1128/mcb.18.5.2789.

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ABSTRACT Mutations in the SEC238 and SRP54 genes of the yeast Yarrowia lipolytica not only cause temperature-sensitive defects in the exit of the precursor form of alkaline extracellular protease and of other secretory proteins from the endoplasmic reticulum and in protein secretion but also lead to temperature-sensitive growth in oleic acid-containing medium, the metabolism of which requires the assembly of functionally intact peroxisomes. The sec238A andsrp54KO mutations at the restrictive temperature significantly reduce the size and number of peroxisomes, affect the import of peroxisomal m

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Mauriac, Stephanie A., Thibault Peineau, Aamir Zuberi, Cathleen Lutz, and Gwénaëlle S. G. Géléoc. "Loss of Pex1 in Inner Ear Hair Cells Contributes to Cochlear Synaptopathy and Hearing Loss." Cells 11, no. 24 (December 9, 2022): 3982. http://dx.doi.org/10.3390/cells11243982.

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Peroxisome Biogenesis Disorders (PBD) and Zellweger syndrome spectrum disorders (ZSD) are rare genetic multisystem disorders that include hearing impairment and are associated with defects in peroxisome assembly, function, or both. Mutations in 13 peroxin (PEX) genes have been found to cause PBD-ZSD with ~70% of patients harboring mutations in PEX1. Limited research has focused on the impact of peroxisomal disorders on auditory function. As sensory hair cells are particularly vulnerable to metabolic changes, we hypothesize that mutations in PEX1 lead to oxidative stress affecting hair cells of

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Saveria, Tracy, André Halbach, Ralf Erdmann, Rudolf Volkmer-Engert, Christiane Landgraf, Hanspeter Rottensteiner, and Marilyn Parsons. "Conservation of PEX19-Binding Motifs Required for Protein Targeting to Mammalian Peroxisomal and Trypanosome Glycosomal Membranes." Eukaryotic Cell 6, no. 8 (June 22, 2007): 1439–49. http://dx.doi.org/10.1128/ec.00084-07.

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ABSTRACT Glycosomes are divergent peroxisomes found in trypanosomatid protozoa, including those that cause severe human diseases throughout much of the world. While peroxisomes are dispensable for both yeast (Saccharomyces cerevisiae and others) and mammalian cells in vitro, glycosomes are essential for trypanosomes and hence are viewed as a potential drug target. The import of proteins into the matrix of peroxisomes utilizes multiple peroxisomal membrane proteins which require the peroxin PEX19 for insertion into the peroxisomal membrane. In this report, we show that the specificity of peroxi

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Min, Kyunghun, Hokyoung Son, Jungkwan Lee, Gyung Ja Choi, Jin-Cheol Kim, and Yin-Won Lee. "Peroxisome Function Is Required for Virulence and Survival of Fusarium graminearum." Molecular Plant-Microbe Interactions® 25, no. 12 (December 2012): 1617–27. http://dx.doi.org/10.1094/mpmi-06-12-0149-r.

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Peroxisomes are organelles that are involved in a number of important cellular metabolic processes, including the β-oxidation of fatty acids, biosynthesis of secondary metabolites, and detoxification of reactive oxygen species (ROS). In this study, the role of peroxisomes was examined in Fusarium graminearum by targeted deletion of three genes (PEX5, PEX6, and PEX7) encoding peroxin (PEX) proteins required for peroxisomal protein import. PEX5 and PEX7 deletion mutants were unable to localize the fluorescently tagged peroxisomal targeting signal type 1 (PTS1)- and PTS2-containing proteins to pe

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Mastalski, Thomas, Rebecca Brinkmeier, and Harald W. Platta. "The Peroxisomal PTS1-Import Defect of PEX1- Deficient Cells Is Independent of Pexophagy in Saccharomyces cerevisiae." International Journal of Molecular Sciences 21, no. 3 (January 29, 2020): 867. http://dx.doi.org/10.3390/ijms21030867.

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The important physiologic role of peroxisomes is shown by the occurrence of peroxisomal biogenesis disorders (PBDs) in humans. This spectrum of autosomal recessive metabolic disorders is characterized by defective peroxisome assembly and impaired peroxisomal functions. PBDs are caused by mutations in the peroxisomal biogenesis factors, which are required for the correct compartmentalization of peroxisomal matrix enzymes. Recent work from patient cells that contain the Pex1(G843D) point mutant suggested that the inhibition of the lysosome, and therefore the block of pexophagy, was beneficial fo

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Rinaldi, Mauro A., Wendell A. Fleming, Kim L. Gonzalez, Jaeseok Park, Meredith J. Ventura, Ashish B. Patel, and Bonnie Bartel. "The PEX1 ATPase Stabilizes PEX6 and Plays Essential Roles in Peroxisome Biology." Plant Physiology 174, no. 4 (June 9, 2017): 2231–47. http://dx.doi.org/10.1104/pp.17.00548.

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Pedrosa, Ana G., Tânia Francisco, Diana Bicho, Ana F. Dias, Aurora Barros-Barbosa, Vera Hagmann, Gabriele Dodt, Tony A. Rodrigues, and Jorge E. Azevedo. "Peroxisomal monoubiquitinated PEX5 interacts with the AAA ATPases PEX1 and PEX6 and is unfolded during its dislocation into the cytosol." Journal of Biological Chemistry 293, no. 29 (June 8, 2018): 11553–63. http://dx.doi.org/10.1074/jbc.ra118.003669.

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Walter, Claudia, Jeannette Gootjes, Petra A. Mooijer, Herma Portsteffen, Christina Klein, Hans R. Waterham, Peter G. Barth, et al. "Disorders of Peroxisome Biogenesis Due to Mutations in PEX1: Phenotypes and PEX1 Protein Levels." American Journal of Human Genetics 69, no. 1 (July 2001): 35–48. http://dx.doi.org/10.1086/321265.

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Tan, Dongyan, Neil B. Blok, Tom A. Rapoport, and Thomas Walz. "Structures of the double-ring AAA ATPase Pex1-Pex6 involved in peroxisome biogenesis." FEBS Journal 283, no. 6 (November 12, 2015): 986–92. http://dx.doi.org/10.1111/febs.13569.

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SKONECZNY, Marek, and Joanna RYTKA. "Oxygen and haem regulate the synthesis of peroxisomal proteins: catalase A, acyl-CoA oxidase and Pex1p in the yeast Saccharomyces cerevisiae; the regulation of these proteins by oxygen is not mediated by haem." Biochemical Journal 350, no. 1 (August 9, 2000): 313–19. http://dx.doi.org/10.1042/bj3500313.

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Saccharomyces cerevisiae genes related to respiration are typically controlled by oxygen and haem. Usually the regulation by these factors is co-ordinated; haem is indicated as the oxygen sensor. However, the responsiveness of peroxisome functions to these regulatory factors is poorly understood. The expression of CTA1, POX1 and PEX1 genes encoding the peroxisomal proteins catalase A, acyl-CoA oxidase and Pex1p peroxin respectively was studied under various conditions: in anaerobiosis, in the absence of haem and in respiratory incompetence caused by the lack of a mitochondrial genome (ρ0). The

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Kiel, J. A. K. W., R. E. Hilbrands, R. A. L. Bovenberg, and M. Veenhuis. "Isolation of Penicillium chrysogenum PEX1 and PEX6 encoding AAA proteins involved in peroxisome biogenesis." Applied Microbiology and Biotechnology 54, no. 2 (August 15, 2000): 238–42. http://dx.doi.org/10.1007/s002530000378.

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34

Di Pietro, Erminia, Catherine Argyriou, Panteha Saberian, Ellen Crushell, Steven Steinberg, Yasmin D’Souza, and Nancy Braverman. "A PEX1 terminal deletion retains partial PEX1 protein function resulting in an attenuated Zellweger spectrum phenotype." Molecular Genetics and Metabolism 132 (April 2021): S164. http://dx.doi.org/10.1016/s1096-7192(21)00344-9.

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35

Mbekeani, Alison, Will Stanley, Vishal Kalel, Noa Dahan, Einat Zalckvar, Lilach Sheiner, Wolfgang Schliebs, Ralf Erdmann, Ehmke Pohl, and Paul Denny. "Functional Analyses of a Putative, Membrane-Bound, Peroxisomal Protein Import Mechanism from the Apicomplexan Protozoan Toxoplasma gondii." Genes 9, no. 9 (August 29, 2018): 434. http://dx.doi.org/10.3390/genes9090434.

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Peroxisomes are central to eukaryotic metabolism, including the oxidation of fatty acids—which subsequently provide an important source of metabolic energy—and in the biosynthesis of cholesterol and plasmalogens. However, the presence and nature of peroxisomes in the parasitic apicomplexan protozoa remains controversial. A survey of the available genomes revealed that genes encoding peroxisome biogenesis factors, so-called peroxins (Pex), are only present in a subset of these parasites, the coccidia. The basic principle of peroxisomal protein import is evolutionarily conserved, proteins harbou

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36

Goto, Shino, Shoji Mano, Chihiro Nakamori, and Mikio Nishimura. "Arabidopsis ABERRANT PEROXISOME MORPHOLOGY9 Is a Peroxin That Recruits the PEX1-PEX6 Complex to Peroxisomes." Plant Cell 23, no. 4 (April 2011): 1573–87. http://dx.doi.org/10.1105/tpc.110.080770.

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37

Gardner, Brooke M., Saikat Chowdhury, Gabriel C. Lander, and Andreas Martin. "The Pex1/Pex6 Complex Is a Heterohexameric AAA + Motor with Alternating and Highly Coordinated Subunits." Journal of Molecular Biology 427, no. 6 (March 2015): 1375–88. http://dx.doi.org/10.1016/j.jmb.2015.01.019.

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38

Ratbi, Ilham, Kim D. Falkenberg, Manou Sommen, Nada Al-Sheqaih, Soukaina Guaoua, Geert Vandeweyer, Jill E. Urquhart, et al. "Heimler Syndrome Is Caused by Hypomorphic Mutations in the Peroxisome-Biogenesis Genes PEX1 and PEX6." American Journal of Human Genetics 97, no. 4 (October 2015): 535–45. http://dx.doi.org/10.1016/j.ajhg.2015.08.011.

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39

Pedrosa, Ana G., Tânia Francisco, Maria J. Ferreira, Tony A. Rodrigues, Aurora Barros-Barbosa, and Jorge E. Azevedo. "A Mechanistic Perspective on PEX1 and PEX6, Two AAA+ Proteins of the Peroxisomal Protein Import Machinery." International Journal of Molecular Sciences 20, no. 21 (October 23, 2019): 5246. http://dx.doi.org/10.3390/ijms20215246.

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In contrast to many protein translocases that use ATP or GTP hydrolysis as the driving force to transport proteins across biological membranes, the peroxisomal matrix protein import machinery relies on a regulated self-assembly mechanism for this purpose and uses ATP hydrolysis only to reset its components. The ATP-dependent protein complex in charge of resetting this machinery—the Receptor Export Module (REM)—comprises two members of the “ATPases Associated with diverse cellular Activities” (AAA+) family, PEX1 and PEX6, and a membrane protein that anchors the ATPases to the organelle membrane

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40

Michelakakis, Helen M., Dimitrios I. Zafeiriou, Marina S. Moraitou, Jeannette Gootjes, and Ronald J. A. Wanders. "PEX1 deficiency presenting as Leber congenital amaurosis." Pediatric Neurology 31, no. 2 (August 2004): 146–49. http://dx.doi.org/10.1016/j.pediatrneurol.2004.01.013.

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41

Gunduz, Mehmet, and Ozlem Unal. "Dysmorphic Facial Features and Other Clinical Characteristics in Two Patients with PEX1 Gene Mutations." Case Reports in Pediatrics 2016 (2016): 1–5. http://dx.doi.org/10.1155/2016/5175709.

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Peroxisomal disorders are a group of genetically heterogeneous metabolic diseases related to dysfunction of peroxisomes. Dysmorphic features, neurological abnormalities, and hepatic dysfunction can be presenting signs of peroxisomal disorders. Here we presented dysmorphic facial features and other clinical characteristics in two patients with PEX1 gene mutation. Follow-up periods were 3.5 years and 1 year in the patients. Case I was one-year-old girl that presented with neurodevelopmental delay, hepatomegaly, bilateral hearing loss, and visual problems. Ophthalmologic examination suggested sep

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42

Guerrero-Solano, José Antonio, Mirandeli Bautista, Josué Vidal Espinosa-Juárez, Luis Alfonso Moreno-Rocha, Gabriel Betanzos-Cabrera, Liana Claudia Salanță, Minarda De la O Arciniega, Elena G. Olvera-Hernández, and Osmar Antonio Jaramillo-Morales. "Differential Antinociceptive Efficacy of Peel Extracts and Lyophilized Juices of Three Varieties of Mexican Pomegranate (Punica granatum L.) in the Formalin Test." Plants 12, no. 1 (December 27, 2022): 131. http://dx.doi.org/10.3390/plants12010131.

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Pharmacological treatment of pain often causes undesirable effects, so it is necessary to look for natural, safe, and effective alternatives to alleviate painful behavior. In this context, it is known that different parts of pomegranate have been widely consumed and used as preventive and therapeutic agents since ancient times. For example, it has been shown to have an antinociceptive effect, however, there are many varieties. Each part has been found to display unique and attractive pharmacological activities. The content of the active phytochemicals in pomegranate depends on the cultivar, ge

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43

Imamura, Atsushi, Nobuyuki Shimozawa, Yasuyuki Suzuki, Zhongyi Zhang, Toshiro Tsukamoto, Yukio Fujiki, Tadao Orii, Takashi Osumi, Ronald J. A. Wanders, and Naomi Kondo. "Temperature-Sensitive Mutation of PEX6 in Peroxisome Biogenesis Disorders in Complementation Group C (CG-C): Comparative Study of PEX6 and PEX1." Pediatric Research 48, no. 4 (October 2000): 541–45. http://dx.doi.org/10.1203/00006450-200010000-00020.

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44

Shiozawa, Kumiko, Nobuo Maita, Kentaro Tomii, Azusa Seto, Natsuko Goda, Yutaka Akiyama, Toshiyuki Shimizu, Masahiro Shirakawa, and Hidekazu Hiroaki. "Crystallographic characterization of the N-terminal domain of PEX1." Acta Crystallographica Section D Biological Crystallography 60, no. 11 (October 20, 2004): 2098–99. http://dx.doi.org/10.1107/s090744490402428x.

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45

Galiani, Silvia, Dominic Waithe, Katharina Reglinski, Luis Daniel Cruz-Zaragoza, Esther Garcia, Mathias P. Clausen, Wolfgang Schliebs, Ralf Erdmann, and Christian Eggeling. "Super-resolution Microscopy Reveals Compartmentalization of Peroxisomal Membrane Proteins." Journal of Biological Chemistry 291, no. 33 (June 16, 2016): 16948–62. http://dx.doi.org/10.1074/jbc.m116.734038.

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Membrane-associated events during peroxisomal protein import processes play an essential role in peroxisome functionality. Many details of these processes are not known due to missing spatial resolution of technologies capable of investigating peroxisomes directly in the cell. Here, we present the use of super-resolution optical stimulated emission depletion microscopy to investigate with sub-60-nm resolution the heterogeneous spatial organization of the peroxisomal proteins PEX5, PEX14, and PEX11 around actively importing peroxisomes, showing distinct differences between these peroxins. Moreo

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46

Pan, Ronghui, John Satkovich, and Jianping Hu. "E3 ubiquitin ligase SP1 regulates peroxisome biogenesis in Arabidopsis." Proceedings of the National Academy of Sciences 113, no. 46 (October 31, 2016): E7307—E7316. http://dx.doi.org/10.1073/pnas.1613530113.

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Peroxisomes are ubiquitous eukaryotic organelles that play pivotal roles in a suite of metabolic processes and often act coordinately with other organelles, such as chloroplasts and mitochondria. Peroxisomes import proteins to the peroxisome matrix by peroxins (PEX proteins), but how the function of the PEX proteins is regulated is poorly understood. In this study, we identified the Arabidopsis RING (really interesting new gene) type E3 ubiquitin ligase SP1 [suppressor of plastid protein import locus 1 (ppi1) 1] as a peroxisome membrane protein with a regulatory role in peroxisome protein impo

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47

TAMURA, Shigehiko, Naomi MATSUMOTO, Atsushi IMAMURA, Nobuyuki SHIMOZAWA, Yasuyuki SUZUKI, Naomi KONDO, and Yukio FUJIKI. "Phenotype‒genotype relationships in peroxisome biogenesis disorders of PEX1-defective complementation group 1 are defined by Pex1p‒Pex6p interaction." Biochemical Journal 357, no. 2 (July 15, 2001): 417. http://dx.doi.org/10.1042/0264-6021:3570417.

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48

Park, Na Yeon, Doo Sin Jo, So Jung Park, Heejin Lee, Ji-Eun Bae, Youlim Hong, Joon Bum Kim, et al. "Depletion of HNRNPA1 induces peroxisomal autophagy by regulating PEX1 expression." Biochemical and Biophysical Research Communications 545 (March 2021): 69–74. http://dx.doi.org/10.1016/j.bbrc.2021.01.083.

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49

Zhang, R., L. Chen, S. Jiralerspong, A. Snowden, S. Steinberg, and N. Braverman. "Recovery of PEX1-Gly843Asp peroxisome dysfunction by small-molecule compounds." Proceedings of the National Academy of Sciences 107, no. 12 (March 8, 2010): 5569–74. http://dx.doi.org/10.1073/pnas.0914960107.

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50

Shiozawa, K., N. Maita, K. Tomii, A. Seto, N. Goda, Y. Akiyama, T. Shimizu, M. Shirakawa, and H. Hiroaki. "Structure of the N-terminal domain of PEX1 AAA-ATPase." Acta Crystallographica Section A Foundations of Crystallography 61, a1 (August 23, 2005): c268. http://dx.doi.org/10.1107/s0108767305088574.

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