Structural insights into the BRAF monomer-to-dimer transition mediated by RAS binding
RAF kinases are essential for RAS protein signalling but how RAS binding regulates dimerization and activation of RAF has remained unclear. Here, the authors report cryoEM structures that provide mechanistic insights into the RAS-mediated monomer-to-dimer transition of full-length BRAF.
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-01-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-28084-3 |
| _version_ | 1819231438640250880 |
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| author | Juliana A. Martinez Fiesco David E. Durrant Deborah K. Morrison Ping Zhang |
| author_facet | Juliana A. Martinez Fiesco David E. Durrant Deborah K. Morrison Ping Zhang |
| author_sort | Juliana A. Martinez Fiesco |
| collection | DOAJ |
| description | RAF kinases are essential for RAS protein signalling but how RAS binding regulates dimerization and activation of RAF has remained unclear. Here, the authors report cryoEM structures that provide mechanistic insights into the RAS-mediated monomer-to-dimer transition of full-length BRAF. |
| first_indexed | 2024-12-23T11:44:58Z |
| format | Article |
| id | doaj.art-34e7836b1f4c4780b3bb919337e7db0b |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-23T11:44:58Z |
| publishDate | 2022-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-34e7836b1f4c4780b3bb919337e7db0b2022-12-21T17:48:22ZengNature PortfolioNature Communications2041-17232022-01-0113111410.1038/s41467-022-28084-3Structural insights into the BRAF monomer-to-dimer transition mediated by RAS bindingJuliana A. Martinez Fiesco0David E. Durrant1Deborah K. Morrison2Ping Zhang3Center for Structural Biology, Center for Cancer Research, National Cancer Institute-FrederickLaboratory of Cell and Developmental Signaling, Center for Cancer Research, National Cancer Institute-FrederickLaboratory of Cell and Developmental Signaling, Center for Cancer Research, National Cancer Institute-FrederickCenter for Structural Biology, Center for Cancer Research, National Cancer Institute-FrederickRAF kinases are essential for RAS protein signalling but how RAS binding regulates dimerization and activation of RAF has remained unclear. Here, the authors report cryoEM structures that provide mechanistic insights into the RAS-mediated monomer-to-dimer transition of full-length BRAF.https://doi.org/10.1038/s41467-022-28084-3 |
| spellingShingle | Juliana A. Martinez Fiesco David E. Durrant Deborah K. Morrison Ping Zhang Structural insights into the BRAF monomer-to-dimer transition mediated by RAS binding Nature Communications |
| title | Structural insights into the BRAF monomer-to-dimer transition mediated by RAS binding |
| title_full | Structural insights into the BRAF monomer-to-dimer transition mediated by RAS binding |
| title_fullStr | Structural insights into the BRAF monomer-to-dimer transition mediated by RAS binding |
| title_full_unstemmed | Structural insights into the BRAF monomer-to-dimer transition mediated by RAS binding |
| title_short | Structural insights into the BRAF monomer-to-dimer transition mediated by RAS binding |
| title_sort | structural insights into the braf monomer to dimer transition mediated by ras binding |
| url | https://doi.org/10.1038/s41467-022-28084-3 |
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