Kurz, T. , Chou, Y.-C., Willems, A. R., Meyer-Schaller, N., Hecht, M.-L., Tyers, M., Peter, M. and Sicheri, F. (2008) Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation. Molecular Cell, 29(1), pp. 23-35. (doi: 10.1016/j.molcel.2007.12.012) (PMID:18206966)
Full text not currently available from Enlighten.
Abstract
Cullin-based E3 ubiquitin ligases are activated through modification of the cullin subunit with the ubiquitin-like protein Nedd8. Dcn1 regulates cullin neddylation and thus ubiquitin ligase activity. Here we describe the 1.9 Å X-ray crystal structure of yeast Dcn1 encompassing an N-terminal ubiquitin-binding (UBA) domain and a C-terminal domain of unique architecture, which we termed PONY domain. A conserved surface on Dcn1 is required for direct binding to cullins and for neddylation. The reciprocal binding site for Dcn1 on Cdc53 is located ∼18 Å from the site of neddylation. Dcn1 does not require cysteine residues for catalytic function, and directly interacts with the Nedd8 E2 Ubc12 on a surface that overlaps with the E1-binding site. We show that Dcn1 is necessary and sufficient for cullin neddylation in a purified recombinant system. Taken together, these data demonstrate that Dcn1 is a scaffold-like E3 ligase for cullin neddylation.
Item Type: | Articles |
---|---|
Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Kurz, Dr Thimo |
Authors: | Kurz, T., Chou, Y.-C., Willems, A. R., Meyer-Schaller, N., Hecht, M.-L., Tyers, M., Peter, M., and Sicheri, F. |
College/School: | College of Medical Veterinary and Life Sciences > School of Molecular Biosciences |
Journal Name: | Molecular Cell |
Publisher: | Elsevier (Cell Press) |
ISSN: | 1097-2765 |
ISSN (Online): | 1097-4164 |
Published Online: | 17 January 2008 |
University Staff: Request a correction | Enlighten Editors: Update this record