A. E. Leschziner

Development of LRRK2 designed ankyrin-repeat proteins

This study develops a high-affinity DARPin that binds to LRRK2's WD40 domain, improving structural analysis and revealing its role in disrupting LRRK2 filaments and Rab8A phosphorylation.

Elf1 promotes Rad26 interaction with lesion-arrested Pol II for transcription-coupled repair

The paper investigates how Rad26 interacts with lesion-arrested Pol II and identifies Elf1's role in enhancing this interaction for transcription-coupled repair.

Inhibition of Parkinsons Disease-related LRRK2 by type-I and type-II kinase inhibitors: activity and structures

This study presents cryo-EM structures of LRRK2 bound to type-I and type-II inhibitors, revealing conformational changes and providing a basis for inhibitor design.

Structure of LRRK1 and mechanisms of autoinhibition and activation

This study solves cryo-EM structures of LRRK1 in monomeric and dimeric forms, revealing distinct autoinhibition mechanisms compared to LRRK2 and their evolutionary context.

Lis1 relieves cytoplasmic dynein-1 auto-inhibition by acting as a molecular wedge

The paper presents a structure showing Lis1 relieves dynein-1 auto-inhibition by acting as a molecular wedge, revealing its role in dynein activation.

Structures of human cytoplasmic dynein in complex with the lissencephaly 1 protein, LIS1

The paper reports cryo-EM structures of human dynein-LIS1 complexes, revealing differences from yeast and mapping disease mutations.

Structural basis for Parkinson's Disease-linked LRRK2's binding to microtubules

This study determines the structural basis of LRRK2's microtubule binding, identifies key residues involved, and shows their disruption affects binding without impacting kinase activity.

Multimodal tubulin binding by the yeast kinesin-8, Kip3, underlies its motility and depolymerization

This study identifies structural features of yeast kinesin-8 Kip3 that enable its switch between motility and MT depolymerization through cryo-EM and molecular dynamics simulations.

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.

Parkinson's Disease-linked LRRK2 structure and model for microtubule interaction

This study reports the structure of LRRK2 and its interaction with microtubules, showing that its conformation regulates binding and affects motor protein function.

A structural mechanism for phosphorylation-dependent inactivation of the AP2 complex

The paper reports cryo-EM structures of NECAP bound to phosphorylated AP2 and shows how phosphorylation marks AP2 for inactivation by NECAP.

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.

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.