KRAS insertion mutations are oncogenic and exhibit distinct functional properties
Amino acid substitutions in K-Ras that constitutively activate the protein are common in cancer. Here, the authors describe mutations in the K-RasSwitch 2 domain and show that the mutant proteins accumulate in the active conformation, exhibit defective binding to PI3 kinase, and are hypersensitive t...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2016-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms10647 |
| _version_ | 1819195066002964480 |
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| author | Yasmine White Aditi Bagchi Jessica Van Ziffle Anagha Inguva Gideon Bollag Chao Zhang Heidi Carias David Dickens Mignon Loh Kevin Shannon Ari J. Firestone |
| author_facet | Yasmine White Aditi Bagchi Jessica Van Ziffle Anagha Inguva Gideon Bollag Chao Zhang Heidi Carias David Dickens Mignon Loh Kevin Shannon Ari J. Firestone |
| author_sort | Yasmine White |
| collection | DOAJ |
| description | Amino acid substitutions in K-Ras that constitutively activate the protein are common in cancer. Here, the authors describe mutations in the K-RasSwitch 2 domain and show that the mutant proteins accumulate in the active conformation, exhibit defective binding to PI3 kinase, and are hypersensitive to MEK inhibitors. |
| first_indexed | 2024-12-23T02:06:50Z |
| format | Article |
| id | doaj.art-c8ee34111da64f238c6f182195674d48 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-23T02:06:50Z |
| publishDate | 2016-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-c8ee34111da64f238c6f182195674d482022-12-21T18:03:52ZengNature PortfolioNature Communications2041-17232016-02-01711810.1038/ncomms10647KRAS insertion mutations are oncogenic and exhibit distinct functional propertiesYasmine White0Aditi Bagchi1Jessica Van Ziffle2Anagha Inguva3Gideon Bollag4Chao Zhang5Heidi Carias6David Dickens7Mignon Loh8Kevin Shannon9Ari J. Firestone10Department of Pediatrics, University of CaliforniaDepartment of Pediatrics, Division of Pediatric Hematology/Oncology and Bone Marrow Transplantation; Helen DeVos Children’s Hospital/Spectrum Health Medical GroupDepartment of Pathology, University of CaliforniaDepartment of Pediatrics, University of CaliforniaPlexxikon IncPlexxikon IncPlexxikon IncDepartment of Pediatrics, Division of Pediatric Hematology/Oncology and Bone Marrow Transplantation; Helen DeVos Children’s Hospital/Spectrum Health Medical GroupDepartment of Pediatrics, University of CaliforniaDepartment of Pediatrics, University of CaliforniaDepartment of Pediatrics, University of CaliforniaAmino acid substitutions in K-Ras that constitutively activate the protein are common in cancer. Here, the authors describe mutations in the K-RasSwitch 2 domain and show that the mutant proteins accumulate in the active conformation, exhibit defective binding to PI3 kinase, and are hypersensitive to MEK inhibitors.https://doi.org/10.1038/ncomms10647 |
| spellingShingle | Yasmine White Aditi Bagchi Jessica Van Ziffle Anagha Inguva Gideon Bollag Chao Zhang Heidi Carias David Dickens Mignon Loh Kevin Shannon Ari J. Firestone KRAS insertion mutations are oncogenic and exhibit distinct functional properties Nature Communications |
| title | KRAS insertion mutations are oncogenic and exhibit distinct functional properties |
| title_full | KRAS insertion mutations are oncogenic and exhibit distinct functional properties |
| title_fullStr | KRAS insertion mutations are oncogenic and exhibit distinct functional properties |
| title_full_unstemmed | KRAS insertion mutations are oncogenic and exhibit distinct functional properties |
| title_short | KRAS insertion mutations are oncogenic and exhibit distinct functional properties |
| title_sort | kras insertion mutations are oncogenic and exhibit distinct functional properties |
| url | https://doi.org/10.1038/ncomms10647 |
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