Z. M. Htet

This study shows Lis1 binding to dynein affects force-induced detachment asymmetry and slows dynein movement without altering stall forces.

This study presents the first high-resolution structure of the yeast dynein-Lis1 complex, revealing molecular interactions essential for Lis1's regulation of dynein function across species.

This study uses single-molecule FRET to show ubiquitin chains regulate proteasome conformational dynamics, enhancing substrate degradation by stabilizing engagement-competent states.

This paper identifies Lis1's role in forming maximally activated dynein complexes by binding to dynein's motor domain, enhancing microtubule binding and velocity.

The paper investigates how molecular motors affect microtubule stability and discovers a self-repair mechanism that counteracts motor-induced damage.

This study reveals that Lis1 regulates cytoplasmic dynein through two opposing modes of microtubule-binding affinity, dependent on Lis1 stoichiometry and dynein's nucleotide state.

The paper identifies ninein and ninein-like as new dynein activators using BioID, revealing their role in cargo binding and motility.