Sushant Suresh

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 identifies ARMH3 as a central scaffold at the Golgi/TGN by defining its interactions with Arl5, PI4KB, and GBF1 using HDX-MS and AI modeling.

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

The paper identifies an unconventional mechanism where Ca2+-CaM binds CHK2 kinase to inhibit its activity, contrasting with its typical role in promoting kinase activity.

This study develops a high-affinity anti-MR1 nanobody that selectively inhibits MR1-restricted T cell activation, providing insights into MR1 function and a tool for immunological research.

The paper reports a cryo-EM structure of EFR3A bound to the PI4KA complex, revealing the molecular mechanism of PI4KA membrane recruitment and its regulation in human disease.

The paper reports a cryo-EM structure of Calcineurin bound to PI4KA, revealing direct interactions with both PI4KA and FAM126A and their conserved binding sequences.