TENT5D

Last update 08 May 2025

Basic Info

Synonyms

CT1.26, CT112, FAM46D

+ [4]

Introduction

Catalyzes the transfer of one adenosine molecule from an ATP to an mRNA poly(A) tail bearing a 3'-OH terminal group.

100 Clinical Results associated with TENT5D

100 Translational Medicine associated with TENT5D

0 Patents (Medical) associated with TENT5D

Literatures (Medical) associated with TENT5D

01 Sep 2024·Andrology

Novel variations in TENT5D lead to teratozoospermia in infertile patients

Article

Author: Wang, Xiang ; Jiang, Chuan ; Yang, Xue ; Zhuo, Liang-Chai ; Wang, Su-Yan ; Yang, Yi-Hong ; Ruan, Tie-Chao ; Shen, Gan ; Zhang, Ying-Teng ; Shen, Ying ; Wang, Yan

AbstractPurposeTeratozoospermia is the main pathogenic factor of male infertility. However, the genetic etiology of teratozoospermia is largely unknown. This study aims to clarify the relationship between novel variations in TENT5D and teratozoospermia in infertile patients.Materials and methodsTwo infertile patients were enrolled. Routine semen analysis of patients and normal controls was conducted with the WHO guidelines. Whole‐exome sequencing (WES) was conducted to identify pathogenic variants in the two patients. Morphology and ultrastructure analysis of spermatozoa in the two patients was determined by Papanicolaou staining, scanning electron microscopy (SEM), and transmission electron microscopy (TEM). The functional effect of the identified variants was analyzed by immunofluorescence staining and western blotting. The expression of TENT5D in different germ cells was detected by immunofluorescence staining.ResultsTwo new hemizygous variations, c.101C > T (p.P34L) and c.125A > T (p.D42V), in TENT5D were detected in two patients with male infertility. Morphology analysis showed abnormalities in spermatozoa morphology in the two patients, including multiple heads, headless, multiple tails, coiled, and/or bent flagella. Ultrastructure analysis showed that most of the spermatozoa exhibited missing or irregularly arranged ‘9+2’ structures. Further functional experiments confirmed the abrogated TENT5D protein expression in patients. In addition, both p.P34L and p.D42V substitutions resulted in a conformational change of the TENT5D protein. We precisely analyzed the subcellular localization of TENT5D in germ cells in humans and mice. And we found that TENT5D was predominantly detected in the head and flagellum of elongating spermatids and epididymal spermatozoa.ConclusionsOur results showed further evidence of a relationship between TENT5D mutation and human male infertility, providing new genetic insight for use in the diagnosis and treatment of male infertility.

01 Sep 2023·Andrology

TENT5D disruption causes oligoasthenoteratozoospermia and male infertility

Article

Author: Sha, Yanwei ; Xiao, Yuwei ; Liu, Wensheng ; Tang, Songxi ; Zhang, Xiaoya ; Xiao, Ziyi ; Zhou, Huiliang ; Wei, Xiaoli ; Deng, Hongjing

AbstractBackgroundOligoasthenoteratozoospermia (OAT) is one of the most complex aggregators of male gametic problems. However, the genetic etiology of OAT is still largely unknown.ObjectivesTo reveal the new genetic factors responsible for male infertility owning to OAT and reveal the outcomes of the affected patients from intracytoplasmic sperm injection (ICSI).Materials and methodsTwo infertile men with typical OAT were recruited in 2018 and retrospected a cohort that included 47 patients with OAT from 2013 to 2021. Fifty healthy men with proven fertility served as control subjects. To identify the novel pathogenic variants, whole‐exome sequencing and Sanger sequencing were used. In silico analysis revealed the affecting of the variants. Field emission scanning electron microscopy was employed to observe the morphological defects of the spermatozoa. Immunofluorescence was used to analyze the expression and localization of the related protein. CRISPR/Cas9 was used to generate the mouse model. ICSI was used as a treatment for the patients and to assess the effects of the pathogenic variant on fertilization and embryo development.ResultsWe identified a loss‐of‐function mutation NM_001170574.2:c.823G > T (p.Glu275*) in X‐linked TENT5D from two patients with OAT. This variant is highly deleterious and has not been found in the human population. The count of patients’ spermatozoa is dramatically decreased and displays multiple morphologic abnormalities with poor motility. Tent5d knockout mice are infertile and exhibit parallel defects. ICSI could rescue the infertility of the Tent5d knockout male mice. Moreover, the proband was treated with ICSI and achieved a successful pregnancy outcome for the first time. Subsequent mutation screening identified no TENT5D mutations among 47 additional patients with OAT and 50 control subjects.ConclusionMutation in TENT5D results in OAT and male infertility, and this terrible situation could be rescued by ICSI.

05 May 2016·Nucleic Acids ResearchQ2 · BIOLOGY

FAM46 proteins are novel eukaryotic non-canonical poly(A) polymerases

Q2 · BIOLOGY

ArticleOA

Author: Kuchta, Krzysztof ; Muszewska, Anna ; Ginalski, Krzysztof ; Wyrwicz, Lucjan S ; Knizewski, Lukasz ; Steczkiewicz, Kamil ; Rychlewski, Leszek ; Pawlowski, Krzysztof

FAM46 proteins, encoded in all known animal genomes, belong to the nucleotidyltransferase (NTase) fold superfamily. All four human FAM46 paralogs (FAM46A, FAM46B, FAM46C, FAM46D) are thought to be involved in several diseases, with FAM46C reported as a causal driver of multiple myeloma; however, their exact functions remain unknown. By using a combination of various bioinformatics analyses (e.g. domain architecture, cellular localization) and exhaustive literature and database searches (e.g. expression profiles, protein interactors), we classified FAM46 proteins as active non-canonical poly(A) polymerases, which modify cytosolic and/or nuclear RNA 3' ends. These proteins may thus regulate gene expression and probably play a critical role during cell differentiation. A detailed analysis of sequence and structure diversity of known NTases possessing PAP/OAS1 SBD domain, combined with state-of-the-art comparative modelling, allowed us to identify potential active site residues responsible for catalysis and substrate binding. We also explored the role of single point mutations found in human cancers and propose that FAM46 genes may be involved in the development of other major malignancies including lung, colorectal, hepatocellular, head and neck, urothelial, endometrial and renal papillary carcinomas and melanoma. Identification of these novel enzymes taking part in RNA metabolism in eukaryotes may guide their further functional studies.

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TENT5D

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