M. S. Cosgrove

This study introduces a point mutation in MLL1 in iPS cells to mimic MLL1F-LSCs phenotypes, revealing that loss of MLL1 enzymatic activity drives H3K4 trimethylation via mislocalized SETd1a.

The paper determines structures of the MLL1-WRAD complex bound to H2B-ubiquitinated nucleosomes using cryo-EM and mass spectrometry-crosslinking, revealing multiple states and the role of ubiquitin in complex assembly.

The paper shows that H3 tail acetylation enhances accessibility of both H3K4 methyl readers and writers, revealing an acetylation-mediated chromatin switch that modulates H3K4 methylation read-write capability.

This study investigates how different polyubiquitin chain lengths and linkages affect UBQLN2's liquid-liquid phase separation, showing that extended chains enhance while compact chains inhibit it.

This study investigates how the MLL1 core complex assembles within biomolecular condensates to regulate H3K4 methylation, proposing a swinging-domain model for spatiotemporal control.