Home > Research > Publications & Outputs > Identification of DHX9 as a cell cycle regulate...

Links

Text available via DOI:

View graph of relations

Identification of DHX9 as a cell cycle regulated nucleolar recruitment factor for CIZ1

Research output: Contribution to journalJournal articlepeer-review

Published

Standard

Identification of DHX9 as a cell cycle regulated nucleolar recruitment factor for CIZ1. / Thacker, U.; Pauzaite, T.; Tollitt, J.; Twardowska, M.; Harrison, C.; Dowle, A.; Coverley, D.; Copeland, N.A.

In: Scientific Reports, Vol. 10, No. 1, 18103, 22.10.2020.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Thacker, U, Pauzaite, T, Tollitt, J, Twardowska, M, Harrison, C, Dowle, A, Coverley, D & Copeland, NA 2020, 'Identification of DHX9 as a cell cycle regulated nucleolar recruitment factor for CIZ1', Scientific Reports, vol. 10, no. 1, 18103. https://doi.org/10.1038/s41598-020-75160-z

APA

Thacker, U., Pauzaite, T., Tollitt, J., Twardowska, M., Harrison, C., Dowle, A., Coverley, D., & Copeland, N. A. (2020). Identification of DHX9 as a cell cycle regulated nucleolar recruitment factor for CIZ1. Scientific Reports, 10(1), [18103]. https://doi.org/10.1038/s41598-020-75160-z

Vancouver

Thacker U, Pauzaite T, Tollitt J, Twardowska M, Harrison C, Dowle A et al. Identification of DHX9 as a cell cycle regulated nucleolar recruitment factor for CIZ1. Scientific Reports. 2020 Oct 22;10(1). 18103. https://doi.org/10.1038/s41598-020-75160-z

Author

Thacker, U. ; Pauzaite, T. ; Tollitt, J. ; Twardowska, M. ; Harrison, C. ; Dowle, A. ; Coverley, D. ; Copeland, N.A. / Identification of DHX9 as a cell cycle regulated nucleolar recruitment factor for CIZ1. In: Scientific Reports. 2020 ; Vol. 10, No. 1.

Bibtex

@article{95fe4de3b9394d9c8d98a3762d7b8fb4,
title = "Identification of DHX9 as a cell cycle regulated nucleolar recruitment factor for CIZ1",
abstract = "CIP1-interacting zinc finger protein 1 (CIZ1) is a nuclear matrix associated protein that facilitates a number of nuclear functions including initiation of DNA replication, epigenetic maintenance and associates with the inactive X-chromosome. Here, to gain more insight into the protein networks that underpin this diverse functionality, molecular panning and mass spectrometry are used to identify protein interaction partners of CIZ1, and CIZ1 replication domain (CIZ1-RD). STRING analysis of CIZ1 interaction partners identified 2 functional clusters: ribosomal subunits and nucleolar proteins including the DEAD box helicases, DHX9, DDX5 and DDX17. DHX9 shares common functions with CIZ1, including interaction with XIST long-non-coding RNA, epigenetic maintenance and regulation of DNA replication. Functional characterisation of the CIZ1-DHX9 complex showed that CIZ1-DHX9 interact in vitro and dynamically colocalise within the nucleolus from early to mid S-phase. CIZ1-DHX9 nucleolar colocalisation is dependent upon RNA polymerase I activity and is abolished by depletion of DHX9. In addition, depletion of DHX9 reduced cell cycle progression from G1 to S-phase in mouse fibroblasts. The data suggest that DHX9-CIZ1 are required for efficient cell cycle progression at the G1/S transition and that nucleolar recruitment is integral to their mechanism of action. ",
author = "U. Thacker and T. Pauzaite and J. Tollitt and M. Twardowska and C. Harrison and A. Dowle and D. Coverley and N.A. Copeland",
year = "2020",
month = oct,
day = "22",
doi = "10.1038/s41598-020-75160-z",
language = "English",
volume = "10",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",
number = "1",

}

RIS

TY - JOUR

T1 - Identification of DHX9 as a cell cycle regulated nucleolar recruitment factor for CIZ1

AU - Thacker, U.

AU - Pauzaite, T.

AU - Tollitt, J.

AU - Twardowska, M.

AU - Harrison, C.

AU - Dowle, A.

AU - Coverley, D.

AU - Copeland, N.A.

PY - 2020/10/22

Y1 - 2020/10/22

N2 - CIP1-interacting zinc finger protein 1 (CIZ1) is a nuclear matrix associated protein that facilitates a number of nuclear functions including initiation of DNA replication, epigenetic maintenance and associates with the inactive X-chromosome. Here, to gain more insight into the protein networks that underpin this diverse functionality, molecular panning and mass spectrometry are used to identify protein interaction partners of CIZ1, and CIZ1 replication domain (CIZ1-RD). STRING analysis of CIZ1 interaction partners identified 2 functional clusters: ribosomal subunits and nucleolar proteins including the DEAD box helicases, DHX9, DDX5 and DDX17. DHX9 shares common functions with CIZ1, including interaction with XIST long-non-coding RNA, epigenetic maintenance and regulation of DNA replication. Functional characterisation of the CIZ1-DHX9 complex showed that CIZ1-DHX9 interact in vitro and dynamically colocalise within the nucleolus from early to mid S-phase. CIZ1-DHX9 nucleolar colocalisation is dependent upon RNA polymerase I activity and is abolished by depletion of DHX9. In addition, depletion of DHX9 reduced cell cycle progression from G1 to S-phase in mouse fibroblasts. The data suggest that DHX9-CIZ1 are required for efficient cell cycle progression at the G1/S transition and that nucleolar recruitment is integral to their mechanism of action.

AB - CIP1-interacting zinc finger protein 1 (CIZ1) is a nuclear matrix associated protein that facilitates a number of nuclear functions including initiation of DNA replication, epigenetic maintenance and associates with the inactive X-chromosome. Here, to gain more insight into the protein networks that underpin this diverse functionality, molecular panning and mass spectrometry are used to identify protein interaction partners of CIZ1, and CIZ1 replication domain (CIZ1-RD). STRING analysis of CIZ1 interaction partners identified 2 functional clusters: ribosomal subunits and nucleolar proteins including the DEAD box helicases, DHX9, DDX5 and DDX17. DHX9 shares common functions with CIZ1, including interaction with XIST long-non-coding RNA, epigenetic maintenance and regulation of DNA replication. Functional characterisation of the CIZ1-DHX9 complex showed that CIZ1-DHX9 interact in vitro and dynamically colocalise within the nucleolus from early to mid S-phase. CIZ1-DHX9 nucleolar colocalisation is dependent upon RNA polymerase I activity and is abolished by depletion of DHX9. In addition, depletion of DHX9 reduced cell cycle progression from G1 to S-phase in mouse fibroblasts. The data suggest that DHX9-CIZ1 are required for efficient cell cycle progression at the G1/S transition and that nucleolar recruitment is integral to their mechanism of action.

U2 - 10.1038/s41598-020-75160-z

DO - 10.1038/s41598-020-75160-z

M3 - Journal article

VL - 10

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

M1 - 18103

ER -