A new NEDD8-ligating system for cullin-4A

Genes Dev. 1998 Aug 1;12(15):2263-8. doi: 10.1101/gad.12.15.2263.

F Osaka ¹, H Kawasaki, N Aida, M Saeki, T Chiba, S Kawashima, K Tanaka, S Kato

Affiliations

Affiliation

1 Kato Cytoprotein Network Project, ERATO, Japan Science and Technology Corporation (JST), Sagami Chemical Research Center, Sagamihara, Kanagawa 229-0012, Japan.

PMID: 9694792 DOI: 10.1101/gad.12.15.2263

Abstract

NEDD8 is a ubiquitin (Ub)-like protein. Here we report a novel ubiquitinylation-related pathway for modification by NEDD8. NEDD8 was activated by an E1 (Ub-activating Enzyme)-like complex, consisting of APP-BP1 and hUba3 with high respective homologies to the amino- and carboxy-terminal regions of E1 and then linked to hUbc12 (a human homolog of yeast Ub-conjugating Enzyme Ubc12p). The major target protein modified by NEDD8 was found to be Hs-cullin-4A (Cul-4A), a member of the family of human cullin/Cdc53 proteins functioning as an essential component of a multifunctional Ub-protein Ligase E3 complex that has a critical role in Ub-mediated proteolysis.

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