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The 3' to 5' exoribonuclease DIS3: from structure and mechanisms to biological functions and role in human disease

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journal contribution
posted on 2023-06-08, 22:31 authored by Sophie R Robinson, Antony OliverAntony Oliver, Timothy ChevassutTimothy Chevassut, Sarah NewburySarah Newbury
DIS3 is a conserved exoribonuclease and catalytic subunit of the exosome, a protein complex involved in the 3’ to 5’ degradation and processing of both nuclear and cytoplasmic RNA species. Recently, aberrant expression of DIS3 has been found to be implicated in a range of different cancers. Perhaps most striking is the finding that DIS3 is recurrently mutated in 11% of multiple myeloma patients. Much work has been done to elucidate the structural and biochemical characteristics of DIS3, including the mechanistic details of its role as an effector of RNA decay pathways. Nevertheless, we do not understand how DIS3 mutations can lead to cancer. There are a number of studies that pertain to the function of DIS3 at the organismal level. Mutant phenotypes in S.pombe, S.cerevisae and Drosophila suggest DIS3 homologues have a common role in cell-cycle progression and microtubule assembly. DIS3 has also recently been implicated in antibody diversification of mouse B-cells. This article aims to review current knowledge of the structure, mechanisms and functions of DIS3 as well as highlighting the genetic patterns observed within myeloma patients, in order to yield insight into the putative role of DIS3 mutations in oncogenesis.

Funding

Epigenetic regulation of gene expression by the exoribonuclease pacman; G0056; BBSRC-BIOTECHNOLOGY & BIOLOGICAL SCIENCES RESEARCH COUNCIL; BB/I021345/1

Ph.D studentship; WC003-14; BSMS; WC003-14

History

Publication status

  • Published

File Version

  • Published version

Journal

Biomolecules

ISSN

2218-273X

Publisher

MDPI

Issue

3

Volume

5

Page range

1515-1539

Department affiliated with

  • BSMS Publications

Research groups affiliated with

  • Haematology Research Group Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2015-09-14

First Open Access (FOA) Date

2015-09-14

First Compliant Deposit (FCD) Date

2015-09-14

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