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- W2274056677 abstract "Cullin-RING ligases (CRL) are ubiquitin E3s that bind substrates through variable substrate-receptor proteins. CRLs are activated by attachment of the ubiquitin-like protein NEDD8 to the Cullin subunit and DCNs are NEDD8 E3 ligases that promote neddylation. Mammalian cells express five DCN-like proteins and little is known about their specific functions or interaction partners. We found that DCNLs form stable stoichiometric complexes with CAND1 and Cullins that can only be neddylated in the presence of substrate adaptor. These DCNL-CUL-CAND1 complexes may represent “reserve” CRLs that can be rapidly activated when needed. We further found that all DCNLs interact with most Cullin subtypes, but that they are likely responsible for the neddylation of different subpopulations of any given Cullin. This is consistent with the fact that the subcellular localization of DCNLs in tissue culture cells differs and that they show unique tissue specific expression patterns in mice. Thus, the specificity between DCNL-type NEDD8 E3 enzymes and their Cullin substrates is only apparent in well-defined physiological contexts and related to their subcellular distribution and restricted expression." @default.
- W2274056677 created "2016-06-24" @default.
- W2274056677 creator A5008364757 @default.
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- W2274056677 date "2016-01-01" @default.
- W2274056677 modified "2023-10-16" @default.
- W2274056677 title "Characterisation of the mammalian family of DCN-type NEDD8 E3 ligases" @default.
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- W2274056677 doi "https://doi.org/10.1242/jcs.181784" @default.
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- W2274056677 hasPublicationYear "2016" @default.
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