NEDD8-UBA3:NAE1 binds a second NEDD8

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

After covalent attachment of the first NEDD8 molecule to the catalytic cysteine, a second NEDD8 binds to the now-free adenylation site on the UBA3 subunit of UBA3:NAE1. This 'doubly-loaded' E1 enzyme is primed to transfer the covalently-bound NEDD8 to the downstream E2 enzyme (Huang et al, 2005; Huang et al, 2007; reviewed in Enchev et al, 2015). Note that although not depicted here, the second NEDD8 moiety is covalently adenylated at its C-terminal glycine residue at the end of this reaction.

Literature References
PubMed ID Title Journal Year
17220875 Basis for a ubiquitin-like protein thioester switch toggling E1-E2 affinity

Huang, DT, Ohi, MD, Hunt, HW, Schulman, BA, Holton, JM, Zhuang, M

Nature 2007
15694336 Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1

Huang, DT, Schulman, BA, Holton, JM, Paydar, A, Waddell, MB, Zhuang, M

Mol. Cell 2005
25531226 Protein neddylation: beyond cullin-RING ligases

Schulman, BA, Enchev, RI, Peter, M

Nat. Rev. Mol. Cell Biol. 2015
Orthologous Events
Cite Us!