Structural mechanism of Myb-MuvB assembly.
Keelan Z GuileyAudra N InessSiddharth SainiSarvind M TripathiJoseph S LipsickLarisa LitovchickSeth M RubinPublished in: Proceedings of the National Academy of Sciences of the United States of America (2018)
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. 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.