GLE1

Last update 08 May 2025

Basic Info

Synonyms

GLE1, GLE1 RNA export mediator, GLE1-like protein

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Introduction

Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC).

100 Clinical Results associated with GLE1

100 Translational Medicine associated with GLE1

0 Patents (Medical) associated with GLE1

104

Literatures (Medical) associated with GLE1

07 Nov 2024·Cureus

The First Case Report of a Homozygous Consensus Acceptor Splice Variant in the NUP214 Gene Associated With Fetal Hydrops and Arthrogryposis Multiplex

Article

Author: Kachhadiya, Tushar ; Vaniawala, Salil ; Vaniawala, Shalin ; Tamhankar, Vasundhara ; Bhammar, Rajesh ; Patel, Jayeshkumar ; Patel, Shwetal ; Tamhankar, Parag M ; Patel, Smit J ; Menon, Pramila

The NUP214 gene encodes a nuclear pore complex protein (nucleoporin, 214 kilodaltons) which plays a critical role in messenger RNA export to the cytoplasm and import of substrates from the cytoplasm. Biallelic mutations in the NUP214 gene have been associated with susceptibility to acute infection-induced encephalopathy type 9 (ILAE9) (Online Mendelian Inheritance in Man (OMIM), 114350), an autosomal recessive disorder. Herein, we describe for the first time, a fetus with hydrops and arthrogryposis multiplex with a homozygous novel consensus splice site variant in the NUP214 gene, chr9:g.131127522A>G or c.46-2A>G (transcript ID NM_005085.4). Parents were heterozygous for the same variant. Mutations in either of 83 genes have been previously published to cause fetal arthrogryposis multiplex but mutations in NUP214 have not been previously reported as per our search in the available medical literature (PubMed/MEDLINE (Medical Literature Analysis and Retrieval System Online) and Google Scholar). STRING (Search Tool for Retrieval of Interacting Genes/Proteins) analysis showed close interactions between NUP214 and the other proteins GLE1, NUP88, NEK9, and THOC2. Thus, this case report expands the phenotype of NUP214 gene-related human disease.

21 Sep 2024·Journal of Biomolecular Structure and Dynamics

Identification of novel nuclear pore complex associated proteins in esophageal carcinoma by an integrated bioinformatics analysis.

Article

Author: Bagheri, Kambiz ; Moghanibashi, Mehdi ; Mohamadynejad, Parisa

Nucleoporins (NUPs) are components of the nuclear pore complex (NPC) that participate in the nucleocytoplasmic transport of macromolecules as well as in many essential processes that may be led to carcinogenesis. We selected three expression profile microarray datasets from GEO and as well as TCGA data to identify differentially expressed NUPs genes in esophageal carcinoma. Our findings indicated that NUP133, NUP37, NUP43, NUP50, GLE1 and NDC1 are overexpressed in esophageal carcinoma, among which NUP50 and GLE1genes are reported for the first time in esophageal carcinoma. All identified NUPs were also associated with distant metastasis.Communicated by Ramaswamy H. Sarma.

01 Dec 2023·Advances in Biological Regulation

Phosphorylation impacts GLE1 nuclear localization and association with DDX1

Article

Author: Sharma, Manisha ; Dawson, T Renee ; Mason, Aaron C ; Wente, Susan R

Gle1 regulates gene expression at multiple steps from transcription to mRNA export to translation under stressed and non-stressed conditions. To better understand Gle1 function in stressed human cells, specific antibodies were generated that recognized the phosphorylation of threonine residue 102 (T102) in Gle1. A series of in vitro kinase assays indicated that T102 phosphorylation serves as a priming event for further phosphorylation in Gle1's N-terminal low complexity cluster. Indirect immunofluorescence microscopy with the anti-Gle1-pT102 antibodies revealed that basally phosphorylated Gle1 was pre-dominantly nuclear with punctate distribution; however, under sodium arsenite-induced stress, more cytoplasmic localization was detected. Immunoprecipitation with the anti-Gle1-pT102 antibody resulted in co-isolation of Gle1-pT102 with the DEAD-box protein DDX1 in a phosphatase sensitive manner. This suggested Gle1 phosphorylation might be linked to its role in regulating DDX1 during transcription termination. Notably, whereas the total Gle1-DDX1 association was decreased when Gle1 nucleocytoplasmic shuttling was disrupted, co-isolation of Gle1-pT102 and DDX1 increased under the same conditions. Taken together, these studies demonstrated that Gle1 phosphorylation impacts its cellular distribution and potentially drives nuclear Gle1 functions in transcription termination. We propose a model wherein phosphorylation of Gle1 either reduces its nucleocytoplasmic shuttling capacity or increases its binding affinity with nuclear interaction partners.

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GLE1

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