Structural mechanism of Myb–MuvB assembly
KZ Guiley, AN Iness, S Saini… - Proceedings of the …, 2018 - National Acad Sciences
Proceedings of the National Academy of Sciences, 2018•National Acad Sciences
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 …
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 …
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.
National Acad Sciences