Structural mechanism of Myb–MuvB assembly
Journal Article
·
· Proceedings of the National Academy of Sciences of the United States of America
- Univ. of California, Santa Cruz, CA (United States)
- Virginia Commonwealth Univ., Richmond, VA (United States)
- Stanford Univ., CA (United States)
The MuvB transcriptional regulatory complex, which controls cell-cycle-dependent gene expression, cooperates with B-Myb to activate genes required for the G2 and M phases of the cell cycle. We have identified the domain in B-Myb that is essential for the assembly of the Myb–MuvB (MMB) complex. We determined a crystal structure that reveals how this B-Myb domain binds MuvB through the adaptor protein LIN52 and the scaffold protein LIN9. Here, the structure and biochemical analysis provide an understanding of how oncogenic B-Myb is recruited to regulate genes required for cell-cycle progression, and the MMB interface presents a potential therapeutic target to inhibit cancer cell proliferation.
- Research Organization:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Organization:
- National Institutes of Health (NIH)
- Grant/Contract Number:
- F31CA206244; R01CA128836; R01CA188571; R01CA132685; R01GM124148
- OSTI ID:
- 1478077
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America, Vol. 115, Issue 40; ISSN 0027-8424
- Publisher:
- National Academy of SciencesCopyright Statement
- Country of Publication:
- United States
- Language:
- ENGLISH
Cited by: 22 works
Citation information provided by
Web of Science
Web of Science
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