Z. M. Htet

Lis1 binding regulates force-induced detachment of cytoplasmic dynein from microtubules

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

Ubiquitin modulates 26S proteasome conformational dynamics and promotes substrate degradation

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

Structural Basis for Cytoplasmic Dynein-1 Regulation by Lis1

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.

Lis1 promotes the formation of maximally activated cytoplasmic dynein-1 complexes

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

Self-repair protects microtubules from their destruction by molecular motors

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

Lis1 has two opposing modes of regulating cytoplasmic dynein

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 Human Cytoplasmic Dynein Interactome Reveals Novel Activators Of Motility

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