Scott D. Hansen

This study shows ECM stiffness enhances EGFR signaling through integrin-mediated membrane curvature and topography, affecting RTK signaling across scales and potentially explaining resistance to tyrosine kinase inhibitors.

This study identifies phosphorylation of Y2090 in PI4KA as an inhibitory mechanism that suppresses its lipid kinase activity through conformational changes and reduced membrane recruitment.

This study shows PIP4K inhibits PIP5K lipid kinase activity by disrupting its membrane-mediated dimerization, maintaining PI(4,5)P2 homeostasis.

This study reconstitutes Ras-PI3Kγ membrane communication and feedback using light-induced signaling inputs, revealing how feedback and diffusion shape spatiotemporal signaling dynamics.

This study identifies two SHIP1 localization modes during neutrophil chemotaxis, regulated by FBP17 and Nck1, and shows that the C-terminal domain is essential for proper chemotaxis.

The paper develops a nanobody that selectively blocks EFR3 recruitment of PI4KA by targeting TTC7B, reducing membrane recruitment and PI4P production.

This study identifies how the SH2 domain sterically occludes the C2 domain to autoinhibit SHIP1, revealing structural and functional relationships critical for its membrane localization and phosphatase activity.

The paper introduces a rapid, inexpensive protocol for mapping nucleosome positions in fungi and mammalian cells, validated across multiple species and compatible with high-throughput sequencing.