14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains
Pohl et al. investigated the structural basis of Nedd4-2 regulation by 14-3-3 and found that phosphorylated Ser342 and Ser448 are the main residues that facilitate 14-3-3 binding to Nedd4-2. The authors propose that the Nedd4-2:14-3-3 complex then stimulates a structural rearrangement of Nedd4-2 thr...
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| Auteurs principaux: | , , , , |
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| Format: | article |
| Langue: | EN |
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Nature Portfolio
2021
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| Accès en ligne: | https://doaj.org/article/28f3af453a79406099b6b0c5ec6e9945 |
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| Résumé: | Pohl et al. investigated the structural basis of Nedd4-2 regulation by 14-3-3 and found that phosphorylated Ser342 and Ser448 are the main residues that facilitate 14-3-3 binding to Nedd4-2. The authors propose that the Nedd4-2:14-3-3 complex then stimulates a structural rearrangement of Nedd4-2 through inhibiting interaction of its structured domains. |
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