Zdeněk Lánský

This study shows tau forms multilayered condensates on microtubules via a prewetting-like transition, creating a selective microenvironment that restricts some proteins while recruiting others.

This study shows that reduced microtubule polyglutamylation causes neuronal dysfunction and worsens Tau-induced neurodegeneration in mice.

The paper designs and characterizes PTX analogues to separate MT stabilization from structural changes, showing that compound 1b preserves native MT structure and physiological Tau dynamics.

This study identifies MTCL1 as a factor linking microtubule stabilization and acetylation, showing its role in neuronal function through molecular mimicry.

This paper investigates how microtubule-stabilizing ligands alter lattice conformation and function, showing they stabilize distinct longitudinal states that affect nucleotide hydrolysis and motor protein interactions.

This study shows that tau phosphorylation impairs the protective function of tau envelopes, leading to microtubule destabilization in neurodegenerative disorders.

This study shows taxanes induce conformational changes in microtubules, releasing GEF-H1 and activating RhoA signaling, leading to actin remodeling.

This study identifies KIF14 as a non-canonical kinesin-3 motor that regulates intraflagellar transport in primary cilia by interacting with its motor domain and C-terminal CC1 domain.

The paper shows that co-polymerization of different tubulin isotypes creates sectioned microtubules that differentially bind MAPs like TPPP1 and OPTN.

The paper uses cell-free assays to show PACRG and FAP20 synergistically stabilize microtubule doublets by reducing B-tubule depolymerization and increasing rescue frequency.

This study identifies OPTN's role in axonal mitochondria transport and shows its loss contributes to neurodegeneration in models of ALS and NTG.

This paper shows FKBP12 inhibits CRMP2A-mediated microtubule polymerization and axon growth by binding to unphosphorylated CRMP2A.

This study shows anillin directly crosslinks microtubules and actin filaments, promoting bundling and sliding, and suggests its role in regulating microtubule-actin crosstalk during cell division.