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Structural mechanism of Myb-MuvB assembly.


ABSTRACT: 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.

SUBMITTER: Guiley KZ 

PROVIDER: S-EPMC6176624 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Structural mechanism of Myb-MuvB assembly.

Guiley Keelan Z KZ   Iness Audra N AN   Saini Siddharth S   Tripathi Sarvind S   Lipsick Joseph S JS   Litovchick Larisa L   Rubin Seth M SM  

Proceedings of the National Academy of Sciences of the United States of America 20180917 40


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 understand  ...[more]

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