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...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2021-07-01
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| Series: | Communications Biology |
| Online Access: | https://doi.org/10.1038/s42003-021-02419-0 |
| _version_ | 1818997153728561152 |
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| author | Pavel Pohl Rohit Joshi Olivia Petrvalska Tomas Obsil Veronika Obsilova |
| author_facet | Pavel Pohl Rohit Joshi Olivia Petrvalska Tomas Obsil Veronika Obsilova |
| author_sort | Pavel Pohl |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-20T21:41:07Z |
| format | Article |
| id | doaj.art-28f3af453a79406099b6b0c5ec6e9945 |
| institution | Directory Open Access Journal |
| issn | 2399-3642 |
| language | English |
| last_indexed | 2024-12-20T21:41:07Z |
| publishDate | 2021-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Communications Biology |
| spelling | doaj.art-28f3af453a79406099b6b0c5ec6e99452022-12-21T19:25:48ZengNature PortfolioCommunications Biology2399-36422021-07-014111510.1038/s42003-021-02419-014-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domainsPavel Pohl0Rohit Joshi1Olivia Petrvalska2Tomas Obsil3Veronika Obsilova4Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of SciencesDepartment of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of SciencesDepartment of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of SciencesDepartment of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of SciencesDepartment of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of SciencesPohl 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.https://doi.org/10.1038/s42003-021-02419-0 |
| spellingShingle | Pavel Pohl Rohit Joshi Olivia Petrvalska Tomas Obsil Veronika Obsilova 14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains Communications Biology |
| title | 14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains |
| title_full | 14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains |
| title_fullStr | 14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains |
| title_full_unstemmed | 14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains |
| title_short | 14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains |
| title_sort | 14 3 3 protein regulates nedd4 2 by modulating interactions between hect and ww domains |
| url | https://doi.org/10.1038/s42003-021-02419-0 |
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