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Title: Structural mechanism of Myb–MuvB assembly

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America

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
Citation Metrics:
Cited by: 22 works
Citation information provided by
Web of Science

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Cited By (2)

A long lost key opens an ancient lock: Drosophila Myb causes a synthetic multivulval phenotype in nematodes journal January 2020
A Cyclin A—Myb-MuvB—Aurora B network regulates the choice between mitotic cycles and polyploid endoreplication cycles journal July 2019