PEX11G

Last update 08 May 2025

Basic Info

Synonyms

Peroxin-11C, peroxisomal biogenesis factor 11 gamma, Peroxisomal biogenesis factor 11C

+ [7]

Introduction

Promotes membrane protrusion and elongation on the peroxisomal surface.

100 Clinical Results associated with PEX11G

100 Translational Medicine associated with PEX11G

0 Patents (Medical) associated with PEX11G

Literatures (Medical) associated with PEX11G

01 Dec 2024·Cellular and Molecular Life Sciences

Dietary cysteine and methionine promote peroxisome elevation and fat loss by induction of CG33474 expression in Drosophila adipose tissue

Article

Author: He, Li ; Liu, Meng

AbstractThe high-protein diet (HPD) has emerged as a potent dietary approach to curb obesity. Peroxisome, a highly malleable organelle, adapts to nutritional changes to maintain homeostasis by remodeling its structure, composition, and quantity. However, the impact of HPD on peroxisomes and the underlying mechanism remains elusive. Using Drosophila melanogaster as a model system, we discovered that HPD specifically increases peroxisome levels within the adipose tissues. This HPD-induced peroxisome elevation is attributed to cysteine and methionine by triggering the expression of CG33474, a fly homolog of mammalian PEX11G. Both the overexpression of Drosophila CG33474 and human PEX11G result in increased peroxisome size. In addition, cysteine and methionine diets both reduce lipid contents, a process that depends on the presence of CG33474. Furthermore, CG33474 stimulates the breakdown of neutral lipids in a cell-autonomous manner. Moreover, the expression of CG33474 triggered by cysteine and methionine requires TOR signaling. Finally, we found that CG33474 promotes inter-organelle contacts between peroxisomes and lipid droplets (LDs), which might be a potential mechanism for CG33474-induced fat loss. In summary, our findings demonstrate that CG33474/PEX11G may serve as an essential molecular bridge linking HPD to peroxisome dynamics and lipid metabolism.Graphical abstractHPD, with cysteine and methionine serving as key amino acids, specifically elevates peroxisome levels in the adipose tissues of Drosophila by inducing CG33474 expression. CG33474/PEX11G performs two essential biological roles in an evolutionarily conserved manner: firstly, overexpression of CG33474/PEX11G leads to increased peroxisome size; secondly, CG33474/PEX11G promotes the breakdown of LDs in a cell-autonomous manner (by strengthening peroxisome-LD interaction). Furthermore, TOR signaling is required for cysteine- and methionine-induced CG33474/PEX11G expression.

01 Feb 2024·Twin Research and Human Genetics

DNA Methylation Mediated the Association of Body Mass Index With Blood Pressure in Chinese Monozygotic Twins

Article

Author: Ning, Feng ; Zhang, Dongfeng ; Yao, Jie ; Wang, Weijing

AbstractObesity is an established risk factor for hypertension, but the mechanisms are only partially understood. We examined whether body mass index (BMI)-related DNA methylation (DNAm) variation would mediate the association of BMI with blood pressure (BP). We first conducted a genomewide DNA methylation analysis in monozygotic twin pairs to detect BMI-related DNAm variation and then evaluated the mediating effect of DNAm on the relationship between BMI and BP levels using the causal inference test (CIT) method and mediation analysis. Ontology enrichment analysis was performed for CpGs using the GREAT tool. A total of 60 twin pairs for BMI and systolic blood pressure (SBP) and 58 twin pairs for BMI and diastolic blood pressure (DBP) were included. BMI was positively associated with SBP (β = 1.86,p= .0004). The association between BMI and DNAm of 85 CpGs reachedp< 1×10–4level. Eleven BMI-related differentially methylated regions (DMRs) withinLNCPRESS1,OGDHL,RNU1-44P,NPHS1,ECEL1P2,LLGL2,RNY4P15,MOGAT3,PHACTR3, andBAI2were found. Of the 85 CpGs, 9 mapped toC10orf71-AS1,NDUFB5P1,KRT80,BAI2,ABCA2,PEX11GandFGF4were significantly associated with SBP levels. Of the 9 CpGs, 2 withinABCA2negatively mediated the association between BMI and SBP, with a mediating effect of −0.24 (95% CI [−0.65, −0.01]). BMI was also positively associated with DBP (β = 0.60,p= .0495). The association between BMI and DNAm of 193 CpGs reachedp< 1×10−4level. Twenty-five BMI-related DMRs withinOGDHL,POU4F2,ECEL1P2,TTC6,SMPD4,EP400,TUBA1CandAGAP2were found. Of the 193 CpGs, 33 mapped toABCA2,ADORA2B,CTNNBIP1,KDM4B,NAA60,RSPH6A,SLC25A19andSTILwere significantly associated with DBP levels. Of the 33 CpGs, 12 withinABCA2,SLC25A19,KDM4B,PTPRN2,DNASE1,TFCP2L1,LMNB2andC10orf71-AS1negatively mediated the association between BMI and DBP, with a total mediation effect of −0.66 (95% CI [−1.07, −0.30]). Interestingly, BMI might also negatively mediate the association between the DNAm of most CpG mediators mentioned above and BP. The mediating effect of DNAm was also found when stratified by sex. In conclusion, DNAm variation may partially negatively mediate the association of BMI with BP. Our findings may provide new clues to further elucidate the pathogenesis of obesity to hypertension and identify new diagnostic biomarkers and therapeutic targets for hypertension.

01 Nov 2017·Journal of Molecular BiologyQ2 · BIOLOGY

A New Yeast Peroxin, Pex36, a Functional Homolog of Mammalian PEX16, Functions in the ER-to-Peroxisome Traffic of Peroxisomal Membrane Proteins

Q2 · BIOLOGY

Article

Author: Stasyk, Oleh V ; Agrawal, Gaurav ; Till, Andreas ; Subramani, Suresh ; Carolino, Krypton ; Hodzic, Zlatan ; Proietto, Marco ; Farré, Jean-Claude ; Stasyk, Olena G ; Sibirny, Andriy A ; Cregg, James

Peroxisomal membrane proteins (PMPs) traffic to peroxisomes by two mechanisms: direct insertion from the cytosol into the peroxisomal membrane and indirect trafficking to peroxisomes via the endoplasmic reticulum (ER). In mammals and yeast, several PMPs traffic via the ER in a Pex3- and Pex19-dependent manner. In Komagataella phaffii (formerly called Pichia pastoris) specifically, the indirect traffic of Pex2, but not of Pex11 or Pex17, depends on Pex3, but all PMPs tested for indirect trafficking require Pex19. In mammals, the indirect traffic of PMPs also requires PEX16, a protein that is absent in most yeast species. In this study, we isolated PEX36, a new gene in K. phaffii, which encodes a PMP. Pex36 is required for cell growth in conditions that require peroxisomes for the metabolism of certain carbon sources. This growth defect in cells lacking Pex36 can be rescued by the expression of human PEX16, Saccharomyces cerevisiae Pex34, or by overexpression of the endogenous K. phaffii Pex25. Pex36 is not an essential protein for peroxisome proliferation, but in the absence of the functionally redundant protein, Pex25, it becomes essential and less than 20% of these cells show import-incompetent, peroxisome-like structures (peroxisome remnants). In the absence of both proteins, peroxisome biogenesis and the intra-ER sorting of Pex2 and Pex11C are seriously impaired, likely by affecting Pex3 and Pex19 function.

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PEX11G

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