C. Patrick Lusk

This study uses DNA-origami rings to investigate FG-Nup interactions and their impact on NPC function, revealing how sequence and post-translational modifications affect protein behavior.

In S. japonicus, the ESCRT adaptor Alx1 activates the essential PH-domain protein Vid27 through interaction, driving postmitotic nuclear envelope sealing independently of Cmp7 and ESCRT-III.

This study shows that O-GlcNAc modification of nucleoporins modulates nuclear pore complex permeability in response to mechanical and osmotic cues.

This study shows that Kms1 and Cbp1 cooperate to ensure accurate homology-directed DNA repair at the nuclear periphery in S. pombe by preventing recombination and incorrect template use.

This study shows that loss of Sun2 reduces extracellular matrix production and prevents lung fibrosis by disrupting nuclear mechanosensing.

This paper introduces a nanobody-based method to detect newly forming nuclear pore complexes in yeast, revealing novel insights into their assembly and localization.

The paper uses a yeast model to identify the nuclear import mechanism of SMAD3, showing that the MH1 domain functions as an importin binding surface.

This paper introduces pan-Expansion Microscopy to visualize nuclear pore complex plasticity, revealing LINC complex-dependent diameter biases and nucleoporin repositioning in an ALS model.

This study quantifies the timeline of nuclear autophagy in yeast, revealing a role for Dnm1 in nuclear envelope remodeling during cargo removal.

The paper investigates how varying the width of DNA origami-based nuclear pore mimics affects permeability, showing that narrower pores restrict viral capsid passage while wider pores allow it with NTR assistance.

This study identifies Kap-β2/Transportin as the nuclear transport receptor for β-catenin in Wnt signaling, showing its role in nuclear import and potential as a therapeutic target.

The paper introduces a DNA-origami NanoTrap to study diffusion barriers formed by FG-nups and finds that motif type, density, and arrangement are critical for barrier effectiveness.

The paper shows LEM domain proteins Heh1 and Heh2 have opposing roles in adaptation through copy number variation and transcriptional induction of genome instability.

The paper shows Heh1 and Chm7 form a nuclear envelope subdomain involved in NPC quality control by recruiting ESCRTs and preventing defective NPC accumulation.