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Literature summary extracted from

  • Mund, T.; Pelham, H.
    Substrate clustering potently regulates the activity of WW-HECT domain-containing ubiquitin ligases (2018), J. Biol. Chem., 293, 5200-5209 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.2.26 ARRDC1 alpha-arrestin, anchoring an ARRDC1-GFP construct to the membrane results in efficient activation and autoubiquitination of NEDD4 ligase Homo sapiens
2.3.2.26 Ndfip2 adaptor protein containing multiple PY domains Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.26 Homo sapiens O00308 isoform WWP2
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.26 [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [Dvl2]-L-lysine
-
 Homo sapiens [E2 ubiquitin-conjugating enzyme]-L-cysteine + [Dvl2]-N6-ubiquitinyl-L-lysine
-
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General Information

EC Number General Information Comment Organism
2.3.2.26 physiological function NEDD4 ligase activation critically requires a substantial array of clustered PY motifs. Soluble protein substrates and adaptors such as alpha-arrestins, even with multiple PY elements, cannot activate ligase activity efficiently. Polymerization or membrane tethering of these substrates dramatically increases the ligase activity both in vivo and in vitro. Aggregation of luciferase-containing substrates upon heat shock has a similar effect and can also expose cryptic PY elements in the substrates Homo sapiens