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The expression of DKC1 was upregulated in ccRCC.
Dyskerin isoform 3 boosts energy metabolism.
dyskerin suppression caused p53-dependent G1 cell-cycle arrest in p53 wild-type cells, and a p53-independent pathway impaired proliferation in cells with p53 dysfunction.
observed dyskerin expression, telomerase RNA accumulation, and pseudouridylation present in all DKC1 mutation carriers at levels comparable to healthy wild-type controls
A mutation in the DC gene 1 (DKC1) at Xq28 results in dysfunction of dyskerin, a protein that is involved in telomere maintenance and ribosomal biogenesis.
Loss of dyskerin binding leads to telomerase RNA component degradation.
Expression of GSE4 increased telomerase activity and reduced DNA damage, oxidative stress and cell senescence in dyskerin-mutated cells.
influence of dyskerin expression on tumor clinical outcome is linked to its role on the maintenance of high levels of TERC
a significant increase in DKC1, RAD50, MRE11 and RPA1 expression in MM cases with high bone marrow infiltration (p=0.03) and a tendency towards cases with advanced ISS stage
Performed a comprehensive study of human dyskerin through structural, phylogenetic and bioinformatic analysis.
DC is genetically heterogeneous. X-linked DC is the commonest form of the disease, accounting for approximately 30% of cases, and is caused by mutations of the DKC1 gene encoding the dyskerin protein.
The non-neoplastic biliary tree seems to progressively lose dyskerin expression from the major branches to the peripheral portal bile ducts. Similarly, intrahepatic cholangiocarcinomas showed two patterns of dyskerin expression
DKC1 mutations were found in Indian patients with aplastic anemia.
dyskerin is a highly dynamic protein throughout the cell cycle and increases the repertoire of fundamental cellular processes that are disrupted by absence of its normal function.
DKC1 variant represents the third telomere-related gene identified as a genetic cause of FIP.
whole-exome sequencing for the genetic diagnosis of this patient with possible Hoyeraal-Hreidarsson syndrome and successfully identified a missense mutation (c.146C>T, p.Thr49Me) in DKC1.
Using human U2OS osteosarcoma cells, the study shows that siRNA-mediated dyskerin depletion induced cellular senescence as evidenced by proliferative arrest, senescence-associated heterochromatinization and a senescence-associated molecular profile.
3 novel alternative splice isoforms of DKC1 derived from human X-linked dyskeratosis congenita 1 have been identified.
that females with heterozygous DKC1 mutations may be at increased risk for developing penetrant telomere phenotypes that, at times, may be associated with clinical morbidity.
Results show that dyskerin stability is regulated by SUMOylation and that mutations altering dyskerin SUMOylation can lead to defects in telomere maintenance that are characteristics of dyskeratosis congenita.
Deficiency in dkc1 and nola1 in the H/ACA RNP complex likely contributes to the hematopoietic phenotype through p53 activation associated with rRNA processing defects during the initial stage of Dyskeratosis congenita pathogenesis.
Mouse embryonic fibroblasts cells with no pseudouridylation activity in H/ACA snoRNPs due to lack of Dkc1, can produce mature ribosomes, however, the ribosomes are very unstable and cell growth and division is very slow.
mTR stability and telomerase activity produced by the Dkc1 A353V mutation in dyskeratosis congenita are rescued by a peptide from the dyskerin TruB domain.
A mouse small nucleolar snoRNA microarray was used to monitor changes in abundance of snoRNAs after ablation of dyskerin, an H/ACA snoRNA protein component, from mouse liver, which causes a decrease in ribosome production.
hepatocytes can survive without dyskerin but the role of dyskerin in RNA modification is essential for cellular proliferation.
Female mice carrying the deletion in the paternally derived Dkc1 show extreme skewing of X-inactivation with the wild type X-chromosome active in all cells.
results establish a role of dyskerin for deregulated rRNA modification in tumor formation and disease pathogenesis in dyskeratosis congenita
Data show that point mutations in dyskerin may affect both the telomerase and pseudouridylation pathways and the extent to which these functions are altered can vary for different mutations.
specific defect in IRES (internal ribosome entry site)-dependent translation in Dkc1 mutant mice; defect results in impaired translation of mRNAs containing IRES elements, including those encoding p27Kip1), Bcl-xL and XIAP
dyskerin mutations cause slow growth independently of telomere shortening and this slow growth is the result of the induction of DNA damage. Thus, dyskerin interacts with telomerase and affects telomere maintenance independently of telomere length.
[CBF5] Arabidopsis CBF5 interacts with NAF1 in planta.
T66A NAP57 behaves as a dominant-negative inhibitor of telomerase. dyskerin is a conserved component of the telomerase RNP complex in higher eukaryotes that is required for maximal enzyme activity in vivo.
This gene is a member of the H/ACA snoRNPs (small nucleolar ribonucleoproteins) gene family. snoRNPs are involved in various aspects of rRNA processing and modification and have been classified into two families: C/D and H/ACA. The H/ACA snoRNPs also include the NOLA1, 2 and 3 proteins. The protein encoded by this gene and the three NOLA proteins localize to the dense fibrillar components of nucleoli and to coiled (Cajal) bodies in the nucleus. Both 18S rRNA production and rRNA pseudouridylation are impaired if any one of the four proteins is depleted. These four H/ACA snoRNP proteins are also components of the telomerase complex. The protein encoded by this gene is related to the Saccharomyces cerevisiae Cbf5p and Drosophila melanogaster Nop60B proteins. The gene lies in a tail-to-tail orientation with the palmitoylated erythrocyte membrane protein gene and is transcribed in a telomere to centromere direction. Both nucleotide substitutions and single trinucleotide repeat polymorphisms have been found in this gene. Mutations in this gene cause X-linked dyskeratosis congenita, a disease resulting in reticulate skin pigmentation, mucosal leukoplakia, nail dystrophy, and progressive bone marrow failure in most cases. Mutations in this gene also cause Hoyeraal-Hreidarsson syndrome, which is a more severe form of dyskeratosis congenita. Two transcript variants encoding different isoforms have been found for this gene.
, H/ACA ribonucleoprotein complex subunit 4
, cbf5p homolog
, nopp140-associated protein of 57 kDa
, nucleolar protein NAP57
, nucleolar protein family A member 4
, snoRNP protein DKC1
, dyskeratosis congenita 1, dyskerin
, H/ACA ribonucleoprotein complex subunit 4-like
, h/ACA ribonucleoprotein complex subunit 4-like
, dyskeratosis congenita 1, dyskerin homolog