| DIS3 depletion in multiple myeloma causes extensive perturbation in cell cycle progression and centrosome amplification. | DIS3 depletion in multiple myeloma causes extensive perturbation in cell cycle progression and centrosome amplification.
Favasuli VK, Ronchetti D, Silvestris I, Puccio N, Fabbiano G, Traini V, Todoerti K, Erratico S, Ciarrocchi A, Fragliasso V, Giannandrea D, Tumiatti F, Chiaramonte R, Torrente Y, Finelli P, Morelli E, Munshi NC, Bolli N, Neri A, Taìana E., Free PMC Article | 01/15/2024 |
| DIS3 Variants are Associated With Primary Ovarian Insufficiency: Importance of Transcription/Translation in Oogenesis. | DIS3 Variants are Associated With Primary Ovarian Insufficiency: Importance of Transcription/Translation in Oogenesis.
Johnstone EB, Gorsi B, Coelho E, Moore B, Farr AM, Cooper AR, Mardis ER, Rajkovic A, Chow CY, Yandell M, Welt CK., Free PMC Article | 08/25/2023 |
| DIS3: The Enigmatic Gene in Multiple Myeloma. | DIS3: The Enigmatic Gene in Multiple Myeloma.
Ohguchi Y, Ohguchi H., Free PMC Article | 03/28/2023 |
| Loss of ribonuclease DIS3 hampers genome integrity in myeloma by disrupting DNA:RNA hybrid metabolism. | Loss of ribonuclease DIS3 hampers genome integrity in myeloma by disrupting DNA:RNA hybrid metabolism.
Gritti I, Basso V, Rinchai D, Corigliano F, Pivetti S, Gaviraghi M, Rosano D, Mazza D, Barozzi S, Roncador M, Parmigiani G, Legube G, Parazzoli D, Cittaro D, Bedognetti D, Mondino A, Segalla S, Tonon G., Free PMC Article | 11/26/2022 |
| MPP6 stimulates both RRP6 and DIS3 to degrade a specified subset of MTR4-sensitive substrates in the human nucleus. | MPP6 stimulates both RRP6 and DIS3 to degrade a specified subset of MTR4-sensitive substrates in the human nucleus.
Fujiwara N, Shigemoto M, Hirayama M, Fujita KI, Seno S, Matsuda H, Nagahama M, Masuda S., Free PMC Article | 09/3/2022 |
| MicroRNA-125a/b-5p promotes malignant behavior in multiple myeloma cells and xenograft tumor growth by targeting DIS3. | MicroRNA-125a/b-5p promotes malignant behavior in multiple myeloma cells and xenograft tumor growth by targeting DIS3.
Zhang T, Wang LL, Guan J, Zhou Y, Cheng P, Zou L. | 06/25/2022 |
| DIS3 mutations in multiple myeloma impact the transcriptional signature and clinical outcome. | DIS3 mutations in multiple myeloma impact the transcriptional signature and clinical outcome.
Todoerti K, Ronchetti D, Favasuli V, Maura F, Morabito F, Bolli N, Taiana E, Neri A., Free PMC Article | 04/9/2022 |
| RNA-regulatory exosome complex confers cellular survival to promote erythropoiesis. | RNA-regulatory exosome complex confers cellular survival to promote erythropoiesis.
Mehta C, Fraga de Andrade I, Matson DR, Dewey CN, Bresnick EH., Free PMC Article | 11/13/2021 |
| BRAF and DIS3 Mutations Associate with Adverse Outcome in a Long-term Follow-up of Patients with Multiple Myeloma. | BRAF and DIS3 Mutations Associate with Adverse Outcome in a Long-term Follow-up of Patients with Multiple Myeloma.
Boyle EM, Ashby C, Tytarenko RG, Deshpande S, Wang H, Wang Y, Rosenthal A, Sawyer J, Tian E, Flynt E, Hoering A, Johnson SK, Rutherford MW, Wardell CP, Bauer MA, Dumontet C, Facon T, Thanendrarajan S, Schinke CD, Zangari M, van Rhee F, Barlogie B, Cairns D, Jackson G, Thakurta A, Davies FE, Morgan GJ, Walker BA. | 02/6/2021 |
| Authors engineered cells in which the 3'-->5' exoribonucleases of the exosome complex, DIS3 and EXOSC10, can be rapidly eliminated to assess their immediate roles in nuclear RNA biology. The loss of DIS3 has the greatest impact, causing the substantial accumulation of thousands of transcripts within 60 min. | Rapid Depletion of DIS3, EXOSC10, or XRN2 Reveals the Immediate Impact of Exoribonucleolysis on Nuclear RNA Metabolism and Transcriptional Control.
Davidson L, Francis L, Cordiner RA, Eaton JD, Estell C, Macias S, Cáceres JF, West S., Free PMC Article | 06/6/2020 |
| The germline variants in DIS3. | Exome sequencing identifies germline variants in DIS3 in familial multiple myeloma.
Pertesi M, Vallée M, Wei X, Revuelta MV, Galia P, Demangel D, Oliver J, Foll M, Chen S, Perrial E, Garderet L, Corre J, Leleu X, Boyle EM, Decaux O, Rodon P, Kolb B, Slama B, Mineur P, Voog E, Le Bris C, Fontan J, Maigre M, Beaumont M, Azais I, Sobol H, Vignon M, Royer B, Perrot A, Fuzibet JG, Dorvaux V, Anglaret B, Cony-Makhoul P, Berthou C, Desquesnes F, Pegourie B, Leyvraz S, Mosser L, Frenkiel N, Augeul-Meunier K, Leduc I, Leyronnas C, Voillat L, Casassus P, Mathiot C, Cheron N, Paubelle E, Moreau P, Bignon YJ, Joly B, Bourquard P, Caillot D, Naman H, Rigaudeau S, Marit G, Macro M, Lambrecht I, Cliquennois M, Vincent L, Helias P, Avet-Loiseau H, Moreno V, Reis RM, Varkonyi J, Kruszewski M, Vangsted AJ, Jurczyszyn A, Zaucha JM, Sainz J, Krawczyk-Kulis M, Wątek M, Pelosini M, Iskierka-Jażdżewska E, Grząśko N, Martinez-Lopez J, Jerez A, Campa D, Buda G, Lesueur F, Dudziński M, García-Sanz R, Nagler A, Rymko M, Jamroziak K, Butrym A, Canzian F, Obazee O, Nilsson B, Klein RJ, Lipkin SM, McKay JD, Dumontet C., Free PMC Article | 02/8/2020 |
| We further demonstrate that polyQ-expanded huntingtin delays Dis3 degradation during heat stress and thus hinders chaperone mRNA stabilization. Our findings not only reveal a post-transcriptional negative feedback loop for maintaining proteostasis, but also uncover a mechanism that contributes to the impaired heat stress response in Huntington's disease | Post-transcriptional negative feedback regulation of proteostasis through the Dis3 ribonuclease and its disruption by polyQ-expanded Huntingtin.
Kong KE, Hung TF, Man PM, Wong TN, Cheng T, Jin DY., Free PMC Article | 12/7/2019 |
| DIS3 isoforms vary in their endoribonuclease activity and are differentially expressed within haematological cancers. | DIS3 isoforms vary in their endoribonuclease activity and are differentially expressed within haematological cancers.
Robinson SR, Viegas SC, Matos RG, Domingues S, Bedir M, Stewart HJS, Chevassut TJ, Oliver AW, Arraiano CM, Newbury SF., Free PMC Article | 04/6/2019 |
| Here, we investigated the interplay of exosome-associated 3'-5' exonucleases DIS3 and RRP6 in rRNA processing and by-product elimination in human cells | Elimination of 01/A'-A0 pre-rRNA processing by-product in human cells involves cooperative action of two nuclear exosome-associated nucleases: RRP6 and DIS3.
Kobyłecki K, Drążkowska K, Kuliński TM, Dziembowski A, Tomecki R., Free PMC Article | 01/12/2019 |
| The 3.8 A resolution cryo-EM structure of the core complex bound to a single-stranded RNA reveals that the RNA channel path is formed by two distinct features of the hDIS3 exoribonuclease: an open conformation and a domain organization more similar to bacterial RNase II than to yeast Rrp44. | Distinct and evolutionary conserved structural features of the human nuclear exosome complex.
Gerlach P, Schuller JM, Bonneau F, Basquin J, Reichelt P, Falk S, Conti E., Free PMC Article | 12/22/2018 |
| Results from a study on gene variability markers in early-stage human embryos shows that DIS3 is a putative variability marker for the 3-day, 8-cell embryo stage, identified by mixture models as well as standard ANOVA. | Variability of Gene Expression Identifies Transcriptional Regulators of Early Human Embryonic Development.
Hasegawa Y, Taylor D, Ovchinnikov DA, Wolvetang EJ, de Torrenté L, Mar JC., Free PMC Article | 07/23/2018 |
| Authors have identified a putative functional indel variant at chr13q22.1 that associates with decreased DIS3 expression in carriers of pancreatic cancer risk-increasing alleles, and could therefore affect nuclear RNA processing and/or decay. | Functional characterization of a chr13q22.1 pancreatic cancer risk locus reveals long-range interaction and allele-specific effects on DIS3 expression.
Hoskins JW, Ibrahim A, Emmanuel MA, Manmiller SM, Wu Y, O'Neill M, Jia J, Collins I, Zhang M, Thomas JV, Rost LM, Das S, Parikh H, Haake JM, Matters GL, Kurtz RC, Bamlet WR, Klein A, Stolzenberg-Solomon R, Wolpin BM, Yarden R, Wang Z, Smith J, Olson SH, Andresson T, Petersen GM, Amundadottir LT., Free PMC Article | 01/20/2018 |
| Data indicate the pathological relevance of exosome component 11 protein (DIS3) mutations in plasma cell dyscrasias and suggest that DIS3 may represent a potential tumor suppressor gene in such disorders. | A compendium of DIS3 mutations and associated transcriptional signatures in plasma cell dyscrasias.
Lionetti M, Barbieri M, Todoerti K, Agnelli L, Fabris S, Tonon G, Segalla S, Cifola I, Pinatel E, Tassone P, Musto P, Baldini L, Neri A., Free PMC Article | 07/30/2016 |
| structure and function of DIS3 | The 3' to 5' Exoribonuclease DIS3: From Structure and Mechanisms to Biological Functions and Role in Human Disease.
Robinson SR, Oliver AW, Chevassut TJ, Newbury SF., Free PMC Article | 03/26/2016 |
| The study establishes that the ribonuclease DIS3, targeting LIN28B, sustains the maturation of let-7 miRNAs and suggests the increased translation of critical oncogenes as one of the biological outcomes of DIS3 inactivation. | The ribonuclease DIS3 promotes let-7 miRNA maturation by degrading the pluripotency factor LIN28B mRNA.
Segalla S, Pivetti S, Todoerti K, Chudzik MA, Giuliani EC, Lazzaro F, Volta V, Lazarevic D, Musco G, Muzi-Falconi M, Neri A, Biffo S, Tonon G., Free PMC Article | 08/22/2015 |
| seven novel somatic DIS3 single nucleotide variants (SNVs) and defined three hot spot mutations within the RNB domain. | The molecular spectrum and clinical impact of DIS3 mutations in multiple myeloma.
Weißbach S, Langer C, Puppe B, Nedeva T, Bach E, Kull M, Bargou R, Einsele H, Rosenwald A, Knop S, Leich E. | 05/16/2015 |
| Overexpression of DIS3 and LRCH1 associated with adenoma to carcinoma progression is linked to the colorectal cancer specific gain of 13q. | Gene-dosage dependent overexpression at the 13q amplicon identifies DIS3 as candidate oncogene in colorectal cancer progression.
de Groen FL, Krijgsman O, Tijssen M, Vriend LE, Ylstra B, Hooijberg E, Meijer GA, Steenbergen RD, Carvalho B. | 08/23/2014 |
| Multiple myeloma-associated hDIS3 mutations interfere with hDIS3 exonucleolytic activity. | Multiple myeloma-associated hDIS3 mutations cause perturbations in cellular RNA metabolism and suggest hDIS3 PIN domain as a potential drug target.
Tomecki R, Drazkowska K, Kucinski I, Stodus K, Szczesny RJ, Gruchota J, Owczarek EP, Kalisiak K, Dziembowski A., Free PMC Article | 03/29/2014 |
| Data show that hDIS3 and hDIS3L are active exonucleases, but only hDIS3 has retained endonucleolytic activity, and suggest that three different ribonucleases can serve as catalytic subunits for the exosome in human cells. | The human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3L.
Tomecki R, Kristiansen MS, Lykke-Andersen S, Chlebowski A, Larsen KM, Szczesny RJ, Drazkowska K, Pastula A, Andersen JS, Stepien PP, Dziembowski A, Jensen TH., Free PMC Article | 08/23/2010 |
| S. cerevisiae Dis3p is identical to Rrp44p, which comprises the exosome involved in ribosomal RNA processing, S. cerevisiae Dis3p was found to be localized in the nucleolus. | Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3.
Shiomi T, Fukushima K, Suzuki N, Nakashima N, Noguchi E, Nishimoto T. | 11/10/2005 |