The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Cancer-Specific Retargeting of BAF Complexes by a Prion-like Domain
Open accessAbstract
SUMMARY Alterations in transcriptional regulators can orchestrate oncogenic gene expression programs in cancer. Here, we show that the BRG1/BRM-associated factor (BAF) chromatin remodeling complex, which is mutated in over 20% of human tumors, interacts with EWSR1, a member of a family of proteins with prion-like domains (PrLD) that are frequent partners in oncogenic fusions with transcription factors. In Ewing sarcoma, we find that the BAF complex is recruited by the EWS-FLI1 fusion protein to tumor-specific enhancers and contributes to target gene activation. This process is a neomorphic property of EWS-FLI1 compared to wild-type FLI1 and depends on tyrosine residues that are necessary for phase transitions of the EWSR1 prion-like domain. Furthermore, fusion of short fragments of EWSR1 to FLI1 is sufficient to recapitulate BAF complex retargeting and EWS-FLI1 activities. Our studies thus demonstrate that the physical properties of prion-like domains can retarget critical chromatin regulatory complexes to establish and maintain oncogenic gene expression programs.
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Metadata
- Authors
- Boulay, G., Sandoval, G. J., Riggi, N., Iyer, S., Buisson, R., Naigles, B., Awad, M. E., Rengarajan, S., Volorio, A., McBride, M. J., Broye, L. C., Zou, L., Stamenkovic, I., Kadoch, C., & Rivera, M. N.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2017-09
- Volume
- 171
- Issue
- 1
- Pages
- 163-178.e19
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2747333975
- Cited by
- 470
- References
- 48
- FWCI
- 13.01
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Boulay, G., Sandoval, G. J., Riggi, N., Iyer, S., Buisson, R., Naigles, B., Awad, M. E., Rengarajan, S., Volorio, A., McBride, M. J., Broye, L. C., Zou, L., Stamenkovic, I., Kadoch, C., & Rivera, M. N. (2017). Cancer-Specific Retargeting of BAF Complexes by a Prion-like Domain. Cell. https://doi.org/10.1016/j.cell.2017.07.036
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