| 1998 |
Overexpression of PEX11β alone is sufficient to induce peroxisome proliferation in the absence of extracellular stimuli, acting through a multistep process involving peroxisome elongation, segregation of PEX11β from other peroxisomal membrane proteins, followed by peroxisome division. |
Overexpression of human PEX11β in mammalian cells with time-course microscopy |
The Journal of biological chemistry |
High |
9792670
|
| 1998 |
PEX11β is a peroxisomal membrane protein whose mRNA levels are similar across all rat tissues examined and are unaffected by peroxisome-proliferating agents, implicating it in constitutive (rather than stimulus-induced) control of peroxisome abundance. |
Northern blot analysis of rat tissues treated with peroxisome proliferators (clofibrate, DEHP) |
The Journal of biological chemistry |
Medium |
9792670
|
| 2012 |
A homozygous nonsense mutation in PEX11β causes an isolated peroxisome division defect without affecting standard peroxisomal metabolic parameters, and the division defect is exacerbated at 40°C correlating with decreased PEX11γ expression. |
Patient fibroblast biochemical/microscopic analysis, Sanger sequencing of PEX11β, temperature-shift experiments |
Journal of medical genetics |
Medium |
22581968
|
| 2012 |
PEX11β, but not PEX11α or PEX11γ, is almost exclusively extracted from peroxisomal membranes of paraformaldehyde-fixed cells by Triton X-100 permeabilization, indicating biochemically distinct membrane association properties of PEX11β compared to other isoforms; loss can be prevented by digitonin permeabilization, glutaraldehyde fixation, or large protein tag (YFP) fusion. |
Detergent extraction assay (Triton X-100 vs digitonin) on PFA-fixed cells, immunofluorescence, western blot of detergent fractions |
Histochemistry and cell biology |
Medium |
22875152
|
| 2011 |
Deletion of both alleles of Pex11β in mice reduces peroxisome number by ~30%, causes increased oxidative stress, delayed neuronal development, and neuronal death; heterozygous deletion (one allele) slightly increases peroxisome abundance yet also causes oxidative stress and partial neuronal death, with partial compensation via SOD2 upregulation. |
Pex11β knockout and heterozygous mouse models; primary neuronal cultures; immunofluorescence; mRNA/protein quantification of neuronal markers; ROS assays |
Disease models & mechanisms |
High |
21954064
|
| 2019 |
Inactivation of PEX11B (via CRISPR-Cas9) does not affect H2O2 permeation across the peroxisomal membrane but unexpectedly leads to partial mislocalization of both peroxisomal membrane and matrix proteins to mitochondria and a decrease in peroxisome density, suggesting a role for PEX11B in peroxisomal protein sorting. |
CRISPR-Cas9 knockout of PEX11B in Flp-In T-REx 293 cells; controlled intracellular H2O2 generation assay; immunofluorescence and subcellular fractionation |
Biochimica et biophysica acta. Biomembranes |
Medium |
31129117
|
| 2022 |
PEX11β can promote peroxisome division in the absence of MFF (mitochondrial fission factor) through a DRP1- and FIS1-dependent alternative pathway; MFF can restore peroxisome morphology in PEX11β-deficient patient cells independently of PEX11β; targeting PEX11β to mitochondria induces mitochondrial division. |
siRNA/shRNA knockdown of MFF, FIS1, DRP1; PEX11β-deficient patient cells; mitochondria-targeted PEX11β constructs; live-cell and fixed immunofluorescence microscopy |
Journal of cell science |
High |
35678336
|
| 2020 |
A functional SMAD2/3 binding site is present in the PEX11β promoter; TGFβ signaling induces peroxisome elongation (a prerequisite for proliferation) and correlates with time-resolved upregulation of PEX11β mRNA but not PEX11α or PEX11γ, placing PEX11β downstream of the TGFβ/SMAD2/3 transcriptional axis. |
Cell-based peroxisome proliferation assay; time-resolved mRNA expression profiling; promoter analysis with SMAD2/3 binding site identification; TGFβ treatment |
Frontiers in cell and developmental biology |
Medium |
33195217
|
| 2022 |
ISOC1 deficiency activates AKT1, and overactivation of AKT1 reduces the stability of PEX11B through protein modification (post-translational), thereby reducing peroxisome biogenesis and affecting inflammatory cytokine production in macrophages. |
ISOC1 siRNA knockdown in LPS-treated RAW264.7 macrophages; AKT1 overexpression/inhibition; PEX11B stability assays; cytokine measurement |
Molecules (Basel, Switzerland) |
Low |
36144632
|
| 2022 |
In fibroblasts from patients deficient in PEX11β (as well as DLP1 and NME3), docosahexaenoic acid (DHA)-containing phospholipids are decreased and arachidonic acid/oleic acid levels are elevated, establishing that PEX11β-dependent peroxisome morphology/dynamics affect phospholipid fatty acid composition. |
Phospholipid composition analysis (lipidomics) of patient fibroblasts (PEX11β-deficient) and Pex11β-KO mouse embryonic fibroblasts |
Journal of inherited metabolic disease |
Medium |
36522796
|
| 2025 |
Palmitic acid (PA) induces palmitoylation of PEX11B at the C25 site, which disrupts PEX11B self-interaction and impedes peroxisome elongation, reducing peroxisomal biogenesis in Schwann cells. |
Acyl-RAC assay and acyl-biotin exchange (ABE) assay for palmitoylation detection; site-directed mutagenesis of C25; laser confocal super-resolution imaging; western blot |
Journal of biomedical science |
Medium |
39934809
|
| 2013 |
Knockdown of Pex11β in Xenopus laevis A6 kidney cells decreases mRNA levels of Pex1, PMP70, and PPARγ, reduces PMP70 protein and peroxisome-like structures, and results in increased cellular H2O2 and mitochondrial reactive oxygen species. |
Morpholino-mediated knockdown; qRT-PCR; immunofluorescence; Amplex Red, DCFDA, and MitoTracker ROS assays |
In vitro cellular & developmental biology. Animal |
Medium |
24234511
|
| 2026 |
PEX11β knockout in human iPSC-derived neural progenitors causes elongated peroxisomal morphology and reduced peroxisomal fission with impaired recruitment of fission proteins, without affecting mitochondrial morphology or respiration; lipidomic analysis showed reduced ether-linked phospholipids in PEX11β-deficient neural progenitors; elongated peroxisomal morphology was independent of the peroxisome-endoplasmic reticulum tether. |
CRISPR/Cas9 knockout of PEX11β in human iPSCs differentiated to neural progenitors and neural rosettes; live imaging; lipidomics; fission protein recruitment assays; mitochondrial respiration measurements |
bioRxivpreprint |
Medium |
41756896
|
| 2025 |
PKC activation promotes PEX11β-dependent peroxisome formation through inactivation of GSK3β, which promotes peroxisome-ER contact site formation; removal of VAPA and VAPB impairs PEX11β-dependent peroxisome biogenesis and PKC regulation. |
PKC activator/inhibitor treatment; GSK3β inhibition; VAPA/VAPB knockdown; live-cell imaging of peroxisome numbers; peroxisome-ER contact site assays |
bioRxivpreprint |
Low |
bio_10.1101_2025.01.21.634043
|
| 2025 |
PEX11B knockout in sheep OA3.Ts cells increases susceptibility to orf virus (ORFV) infection; mechanistically, PEX11B loss disrupts peroxisomal integrity and lipid metabolism, leading to increased plasma membrane fluidity that promotes viral entry and replication. |
Genome-wide CRISPR knockout screen in sheep OA3.Ts cells; PEX11B KO validation; viral infection assays; membrane fluidity measurements; lipid metabolism analysis |
bioRxivpreprint |
Low |
bio_10.1101_2025.11.28.691156
|