AI Article Synopsis
- The study found that knocking down DCUN1D3 hinders S phase progression after UV exposure by increasing p27 protein levels.
- Through experiments, it was discovered that DCUN1D3 interacts with CAND1, and their combined effects prevent S phase progression.
- The absence of DCUN1D3 reduces Cullin-1 neddylation, which disrupts the SCFSKP2 complex that normally targets p27, leading to a buildup of p27 and subsequently blocking the S phase.
Article Abstract
Our previous study showed that knockdown the endogenous expression of DCUN1D3 (also called SCCRO3 or DCNL3) blocked the S phase progression after UV irradiation. Here, we show that the silence of DCUN1D3 can increase the cyclin-dependent kinase inhibitor p27 protein levels after UV irradiation. Through Co-immunoprecipitation experiments, we found that DCUN1D3 bound to CAND1. And DCUN1D3 knockdown synergized with CAND1 over-expression in arresting the S phase. Given the CAND1's established role in Cullin-1 neddylation, we found Cullin-1 was less neddylated in DCUN1D3 deficient cells. So the silence of DCUN1D3 can inhibit the formation of SCFSKP2 complex by reducing Cullin-1 neddylation. Given that p27 is the primary target of SCFSKP2 complex, the cells lost DCUN1D3 showed a remarkable accumulation of p27 to cause S phase block.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5295445 | PMC |
| http://dx.doi.org/10.18632/oncotarget.11302 | DOI Listing |
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Article Synopsis
- The study found that knocking down DCUN1D3 hinders S phase progression after UV exposure by increasing p27 protein levels.
- Through experiments, it was discovered that DCUN1D3 interacts with CAND1, and their combined effects prevent S phase progression.
- The absence of DCUN1D3 reduces Cullin-1 neddylation, which disrupts the SCFSKP2 complex that normally targets p27, leading to a buildup of p27 and subsequently blocking the S phase.
Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.
J Cell Sci
April 2016
Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK
Cullin-RING ligases (CRL) are ubiquitin E3 enzymes that bind substrates through variable substrate receptor proteins and are activated by attachment of the ubiquitin-like protein NEDD8 to the cullin subunit. DCNs are NEDD8 E3 ligases that promote neddylation. Mammalian cells express five DCN-like (DCNL) proteins but little is known about their specific functions or interaction partners.
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