Regulation of mitotic exit by the RNF8 ubiquitin ligase

Plans, Vanessa; Guerra-Rebollo, Marta; Thomson, Timothy M.

doi:10.1038/sj.onc.1210782

Cited by 41 publications

(42 citation statements)

References 28 publications

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“…These effects are consistent with delayed and abortive cytokinesis. [36][37][38] Overall, the number of midbodies in Nup153-depleted cells was twice that of control cells (Fig. 7F).…”

Section: Resultsmentioning

confidence: 95%

The nucleoporin Nup153 affects spindle checkpoint activity due to an association with Mad1

Lussi¹,

Shumaker²,

Shimi³

et al. 2010

Nucleus

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“…These effects are consistent with delayed and abortive cytokinesis. [36][37][38] Overall, the number of midbodies in Nup153-depleted cells was twice that of control cells (Fig. 7F).…”

Section: Resultsmentioning

confidence: 95%

The nucleoporin Nup153 affects spindle checkpoint activity due to an association with Mad1

Lussi¹,

Shumaker²,

Shimi³

et al. 2010

Nucleus

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“…6D), as reported for their S. pombe counterparts (10). We further note that, while this article was under review, another group also reported that DMA1/RNF8 regulates mitotic exit (23). Interestingly, depletion of DMA1/RNF8 compromised the ability of nocodazole-treated cells to maintain mitotic arrest in prometaphase/metaphase, although the MEN, which is inhibited by DMA1/RNF8, is thought to be activated later in mitosis.…”

Section: Discussionmentioning

confidence: 99%

Defective in Mitotic Arrest 1/Ring Finger 8 Is a Checkpoint Protein That Antagonizes the Human Mitotic Exit Network

Tuttle

Bothos

Summers

et al. 2007

Molecular Cancer Research

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A molecular pathway homologous to the S. cerevisiae mitotic exit network (MEN) and S. pombe septation initiation network has recently been described in higher eukaryotes and involves the tumor suppressor kinase LATS1 and its subunit MOB1A. The yeast MEN/septation initiation network pathways are regulated by the ubiquitin ligase defective in mitotic arrest 1 (Dma1p), a checkpoint protein that helps maintain prometaphase arrest when cells are exposed to microtubule poisons. We identified here the RING domain protein ring finger 8 (RNF8) as the human orthologue of the yeast protein Dma1p. Like its yeast counterparts, human DMA1/RNF8 localized at the midbody and its depletion by siRNA compromised mitotic arrest of nocodazole-treated cells in a manner dependent on the MEN. Depletion of MAD2, a spindle checkpoint protein, also compromised mitotic arrest, but in a MEN-independent manner. Thus, two distinct checkpoint pathways maintain mitotic arrest in cells exposed to microtubule poisons.

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“…35 Our discovery that RNF8 is involved in PCNA ubiquitination now extends its potential functions into the DDT pathway. The latter is an S-phase checkpoint response that is activated by DNA damage caused by UV and other genotoxic agents.…”

Section: Discussionmentioning

confidence: 99%

PCNA is ubiquitinated by RNF8

Zhang¹,

Chea²,

Xiao³

et al. 2008

Cell Cycle

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The ubiquitination of PCNA is an essential event in the operation of the DNA Damage Tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. This pathway allows the bypass of DNA damage by translesion synthesis that would otherwise cause replication fork stalling. PCNA is mono-ubiquitinated by Rad18-Rad6, and polyubiquitinated by Rad5-Ubc13/Uev1 in the DDT pathway. Mono-and polyubiquitination of PCNA are key processes in the translesion bypass and template switching sub-pathways of the DDT. DNA damage by IR causes DSBs, which trigger the DNA Damage Response (DDR). The ubiquitin ligase RNF8 has a critical role in the assembly of BRCA1 complexes at the DSBs in the DDR. We show that RNF8 readily mono-ubiquitinates PCNA in the presence of UbcH5c, and polyubiquitinates PCNA in the added presence of Ubc13/Uev1a. These reactions are the same as those performed by Rad18-Rad6 and Rad5-Ubc13. RNF8 depletion suppressed both UV and MNNG-stimulated mono-ubiquitination of PCNA, revealing that an RNF8-dependent pathway for PCNA ubiquitination is operative in vivo. These findings provide evidence that RNF8, a key E3 ligase in the DDR, may also play a role in the DDT.

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Regulation of mitotic exit by the RNF8 ubiquitin ligase

Cited by 41 publications

References 28 publications

The nucleoporin Nup153 affects spindle checkpoint activity due to an association with Mad1

The nucleoporin Nup153 affects spindle checkpoint activity due to an association with Mad1

Defective in Mitotic Arrest 1/Ring Finger 8 Is a Checkpoint Protein That Antagonizes the Human Mitotic Exit Network

PCNA is ubiquitinated by RNF8

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