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neddylation

Nedd8 is a ubiquitin-like small protein modifier. The Nedd8 conjugation process, called neddylation, is similar to ubiquitination. neddylation utilizes the E1 activating-enzyme complex composed of two subunits, APP-BP1 and UBA3, and the E2 conjugating-enzyme, UBC12 (Yeh, 2000). The only known substrates of neddylation are Cullin family proteins -- Cul1, Cul2, Cul3, Cul4A, Cul4B, and Cul5 -- which have been shown to be modified by Nedd8 in mammalian Cells. Cullins directly interact with Roc1, a Ring finger protein, and the Cullin-Roc1 complex comprises the core module of a series of ubiquitin E3 ligases, which confer substrate specificity and therefore regulate the degradation process. Among Cullins, many studies focused on Cul1, an essential component of the SCF complex which functions as ubiquitin E3 ligase. The SCF complex consists of core subunits: Skp1, Cul1/Cdc53, Roc1/Hrt/Rbx1, and a substrate-recognition F-box protein. Cul1 functions as a scaffold protein within the SCF complex; the N-terminal domain of Cul1 interacts with the adaptor protein Skp1 that links with the F-box protein, and the C-terminal domain interacts with Roc1 and the ubiquitin E2 enzyme (Ou, 2002 and references therein). in vitro, neddylation of Cul1 is required for ubiquitination of IkappaBalpha and p27Kip1 (Morimoto, 2000; Podust, 2000; Read, 2000). In addition, neddylation enhances E2-ubiquitin recruitment to SCF. In fission yeast, Nedd8 is essential for the SCF-mediated degradation of Rum-1, a cyclin-dependent kinase inhibitor. In Arabidopsis thaliana, the Nedd8 pathway is required for SCF-mediated auxin response. In mice deficient for UBA3, a subunit of the E1 enzyme in neddylation, embryonic development is aberrant, with accumulation of

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