V600E B-Raf Requires the Hsp90 Chaperone for Stability and Is Degraded in Response to Hsp90 Inhibito...
V600E B-Raf Requires the Hsp90 Chaperone for Stability and Is Degraded in Response to Hsp90 Inhibitors
About this item
Full title
Author / Creator
Grbovic, O. M. , Basso, A. D. , Sawai, A. , Ye, Q. , Friedlander, P. , Solit, D. and Rosen, N.
Publisher
United States: National Academy of Sciences
Journal title
Language
English
Formats
Publication information
Publisher
United States: National Academy of Sciences
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Scope and Contents
Contents
The Raf family includes three members, of which B-Raf is frequently mutated in melanoma and other tumors. We show that Raf-1 and A-Raf require Hsp90 for stability, whereas B-Raf does not. In contrast, mutated, activated B-Raf binds to an Hsp90-cdc37 complex, which is required for its stability and function. Exposure of melanoma cells and tumors to...
Alternative Titles
Full title
V600E B-Raf Requires the Hsp90 Chaperone for Stability and Is Degraded in Response to Hsp90 Inhibitors
Authors, Artists and Contributors
Author / Creator
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Primary Identifiers
Record Identifier
TN_cdi_proquest_miscellaneous_17474089
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_17474089
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.0609973103
