Ask about this productRelated genes to: GLE1 antibody
- Gene:
- GLE1 NIH gene
- Name:
- GLE1 RNA export mediator
- Previous symbol:
- GLE1L, LCCS1
- Synonyms:
- hGLE1
- Chromosome:
- 9q34.11
- Locus Type:
- gene with protein product
- Date approved:
- 1998-06-18
- Date modifiied:
- 2019-04-23
Related products to: GLE1 antibody
Related articles to: GLE1 antibody
- The study aimed to identify key genes related to lipid metabolism in chronic sinusitis and understand their biological implications, considering the growing interest in the association between chronic sinusitis - a complex inflammatory condition - and lipid metabolism due to lipids' role in inflammation and immunity. - Source: PubMed
Publication date: 2025/07/30
Xiong PanhuiLiu LeiPi JingtingWang JiLu TaoKe XiaJiang YuShen YangYang Yucheng - The mRNA export factor GLE1 protein plays critical yet enigmatic functions in RNA processing and has been linked with multiple developmental disorders, including lethal congenital contracture syndrome 1 (LCCS1). Using in vivo genetic engineering to study disturbed GLE1 functions under physiological conditions, we demonstrate that total inactivation of GLE1 results in disorganization of the blastocyst inner cell mass and early embryonic lethality due to defects in lineage specification. In contrast, the knock-in mice genocopying the LCCS1-associated GLE1 variant (Gle1) survive the prenatal period but die suddenly at midadulthood. Gle1 mice present an irregular count and distribution of spinal motor neurons as well as impaired development of neural crest-derived tissues, as demonstrated by defects in the sympathetic innervation of heart ventricles, irregularities in the paravertebral sympathetic ganglia volume, and decreased adrenal chromaffin cell counts. Unlike previously reported for yeast and HeLa cells, analysis of the molecular consequences of the GLE1 variant identified normal poly(A) + RNA distribution in Gle1 cells; however, cells were impaired in RNA and protein synthesis and simultaneously showed severely disturbed formation of G3BP stress granule assembly factor 1 (G3BP1)-positive stress granules. Intriguingly, stressed Gle1 cells show microRNA profiles indicative of impaired transcription, protein metabolism, nervous system development, and axon guidance, further corroborating our functional findings. Our results show the necessity of functional GLE1 for life and indicate that LCCS1 etiology is a result of the pathogenic GLE1 variant impinging differentiation of neural crest derivatives and leading to complex multiorgan defects. - Source: PubMed
Publication date: 2025/07/17
Zárybnický TomášLindfors SonjaMetso SaanaKoivula JuliaSzabo ZoltanValtonen RasmusTulppo MikkoMagga JohannaSaarimäki SamuBläuer SonjaMiinalainen IlkkaKerkelä RistoPiepponen Petteri TVoikar VooteleVäänänen JuhoKivelä RiikkaYadav BhagwanLindgren HannaMattila PirkkoZhang Fu-PingSipilä PetraHinttala ReettaKuure Satu - Liquid-liquid phase separation (LLPS) is the membrane-less formation of functional assemblies from specific molecules. It plays a key role in tumor growth by governing gene expression. This study aims to identify LLPS-associated molecular subtypes and prognostic biomarkers in gastric cancer (GC). - Source: PubMed
Publication date: 2025/05/30
Liu DonghuiLiu MingzhuDu Juan - In recent years, the seed amplification assay (SAA) has enabled the identification of pathological TDP-43 in the cerebrospinal fluid (CSF) and olfactory mucosa (OM) of patients with genetic forms of frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS). Here, we investigated the seeding activity of TDP-43 in OM samples collected from patients with sporadic ALS. - Source: PubMed
Publication date: 2025/04/26
Vizziello MariaDellarole Ilaria LindaCiullini AriannaPascuzzo RiccardoLombardo AnnalisaBellandi FlorianaCelauro LuigiBattipaglia ClaudiaCiusani EmilioRizzo AmbraCatania MarcellaDevigili GraziaDella Seta Sara AdrianaMargiotta ValentinaConsonni MonicaFaltracco VeronicaTiraboschi PietroRiva NiloPortaleone Sara Maria SilviaZanusso GianluigiLegname GiuseppeLauria GiuseppeDalla Bella EleonoraModa Fabio - Despite the exciting progress of bifunctional degrader molecules, also known as proteolysis-targeting chimeras (PROTACs), the rapidly expanding field is still significantly hampered by the lack of available E3 ligase ligands. Our research bridges this gap by uncovering a series of small-molecule ligands to the E3 ligase TRIM21 through DNA-Encoded Library (DEL) technology. We confirmed their interaction with TRIM21 using crystallography and demonstrated their antiproliferative effects across various cancer cell types. Furthermore, proteomic studies identified that the mRNA Export Factor GLE1 and the Nuclear Pore Complex Protein NUP155 were significantly downregulated on TRIM21 ligand treatment. This degradation required TRIM21 and was ubiquitin-proteasome-dependent. More specifically, NUP155 was the primary target for the TRIM21 ligands, while GLE1 was considered a passenger target on initial degradation of NUP155. Using immunofluorescence techniques, we further demonstrated that the degradation of GLE1 and NUP155 proteins impaired the integrity of the nuclear envelope, leading to cell death. Highlighted by this research, a novel mode of action has been discovered for the TRIM21 E3 ligase ligand, acting as a monovalent degrader that triggers de novo interaction with functional complex proteins and induces their degradation. - Source: PubMed
Publication date: 2025/04/18
Li XiaomeiWang QingyangGuo AnpingQiu YapingChen QiuxiaLi YouZhang LanjunGuo YaxinMeng XiaoyunLi ShiqianLiu GuizhiZhang LiyunLiu JianLi XianyangCai LongyingCheng XueminLiu ChuanWang XiaotaoWood AndrewMurray JamesLiu GuansaiLi JinHuang XiaodongDou Dengfeng