Samara L. Reck‐Peterson

This study identifies 'unlatching' as a common mechanism for Parkinson's disease-associated LRRK2 variants, showing increased membrane localization and decreased S935 phosphorylation.

This study shows that endosome motility in Aspergillus species affects light-responsive development and secondary metabolite production.

This paper elucidates the structural mechanisms by which LRRK2 is activated and autoinhibited, showing how mutations affect these processes and suggesting therapeutic strategies.

This study characterizes the molecular architecture of tunneling nanotubes (TNTs) using live-cell imaging and cryo-ET, revealing a complex structure with actin, microtubules, and organelles.

This study uses proximity labeling and phosphoproteomics to analyze LRRK1 and LRRK2 interactomes and phosphorylation sites, identifying novel substrates and the impact of inhibitors.

The paper identifies novel kinase:Rab pairs and characterizes substrate recognition determinants for Rab phosphorylation by kinases like LRRK2.

The paper uses cryo-EM to identify an early intermediate state in dynein activation by LIS1, termed Pre-Chi, and shows its functional importance through mutational analysis.

Hybrid type-II inhibitors RN277 and RN341 target inactive LRRK2 with far fewer kinase off-targets than Rebastinib, preserve S935 phosphorylation, and rescue kinesin motility in vitro.

The paper uses cryo-EM to visualize intermediate states of dynein activation pathway by analyzing structures of dynein and dynein-Lis1 bound to ATP.

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.

This study identifies RNA recoding in cephalopods that enhances kinesin function in response to cold and reveals tissue-specific variants with distinct motile properties.